1 Flashcards
Cell Theory
All organisms are composed of cells
Cells are the basic unit of life
All cells come from preexisting
*viruses are not composed of cells, not an organism
Eukaryotic
membrane bound organelles, capable of mitosis
*mature red blood cells don’t have nuclei, expel it during maturation process
Prokaryotes vs Eukaryotes
Prokaryotes: 1 circular DNA chromosome
Eukaryotes: many linear chromosomes composed of chromatin, nucleus held by double phospholipid membrane (nuclear envelope) which is porous
- Pores are protein complexes which allow exchange of biomolecules (RNA, protein)
Nucleoli
Dense regions in nucleus which assemble ribosomes
Cytoplasm
Contains organelles suspended in cytosol, where sub cellular components are trafficked.
Endosymbiotic Theory
Mitochondria arose when a bacterium was engulfed by another cell and used for energy
Mitochondria
Contain circular mtDNA that make some proteins
Maternally inherited, all mitochondria come from egg
- Cell can contain thousands, mutations in mtDNA lead to serious disorders
- Replicate via binary fission independently of cell like bacteria, DNA replicated and cell splits
Powerhouse of the cell, make cells energy

Mitochondrial Matrix: what processes occur?
Makes ATP using citric acid (Krebs) cycle
- Electron transport chain and ATP synthase embedded in inner membrane
- Inner membrane invaginate (folds back on itself to form pouch) as cristae (increases surface area)
Endoplasmic Reticulum (ER)
continuous with nuclear envelope
Rough and Smooth ER
calcium storage, protein synthesis and lipid metabolism.
Rough ER
Ribosomes embedded which synthesize proteins fed to rough ER for 3D folding and modification
- Glycosylation: add carbohydrate group
- Proteolytic cleavage
- Disulfiide bridges
Membrane bound ribosomes usually form secreted proteins/membrane bound proteins
- Free ribosomes in cytoplasm synthesize intracellular proteins
Smooth ER
- No ribosomes
- lipid metabolism
- steroid hormone precursor synthesis (cholesterol)
- detoxification (liver cells have extensive smooth ER)
- stores calcium in muscle cells for contraction
synthesizes lipids, phospholipids as in plasma membranes, and steroids. Cells that secrete these products, such as cells of the testes, ovaries, and skin oil glands, have an excess of smooth endoplasmic reticulum.

Golgi apparatus (post office)
Once protein is synthesized, packaged into vesicles and sent to Golgi apparatus (post office)
- chambers called cisternae
- receives transport vesicles at cis face, modifies them and send to trans face, then they leave

Lysosome
garbage disposal, extracellular stuff enters cell through endocytosis
- vesicle pinches off from cell membrane then fuses with lysosome
Autophagy: intracellular waste fuse with lysosome for degradation
- Digestive enzymes in lysosomes function at acidic pH, pH of cytoplasm is basic so they can’t function
Peroxisome
Accumulates and neutralizes peroxides, protect against oxidative stress
- *- Peroxides:** generate reactive oxygen species harmful to the cell
- Peroxisome breaks down fatty acids through beta oxidation
- Formed in ER

Cytoskeleton fibers (3 types)
Fibers that act as structure
- Microfilaments (smallest)
- Microtubules
- Intermediate filaments (largest)
Microfilaments
Two intertwined strands of actin polymers (F-actin)
- single actin monomer is a globular protein called G-actin
Cell movement and formation of cleavage furrow (indentation of the cell’s surface that begins the progression of cleavage) and interact with protein myosin to initiate muscle contraction
Polar
Microtubules
wider, polymers of a-tubulin and B-tubilin
- Maintain structural integrity of cell
- Highways for motor proteins to traffic vesicles
- Form mitotic spindles (separate chromosomes)
- In Eukaryotic flagellum and cilia, involved in cell motility
Polar
Kinesin
Traffics vesicles OUTWARD of cell
Dynein
Traffics vesicles INWARD
Centrosomes
Composed of two centrioles, microtubule organizing centers
Flagellum
Tail of cells such as sperm, moves back and forth powered by ATP in Eukaryotes to move
*In Prokaryotes, use rotary motion and powered by proton gradient, composed of flagellin protein and not microtubules
Cilia
Help move substances along cell surface
ex. in lungs cilia help clear out mucus and line Fallopian tubes (egg –> uterus)
Polarity of microtubules and microfilaments
Used for polymerization and depolymerization, adding monomers to positive end and removing from negative end
- Treadmilling: both at same time
Capping proteins
Halt polymerization, prevents growth and shrinkage
Intermediate filaments
Melting pot of protein polymers that provide structural support to cell
- Cell to cell adhesion processes
- *Lamin:** intermediate filament that provides structural support to nucleus
- *Keratin:** hair, skin, nails
1 amu =
1 Dalton = 1.66E-27 kg
Mass of one proton/one neutron
Electrons
Magnitude of charge is equal to 1.6E-19 Coulombs
Electrons closest to nucleus are lowest in energy, most
stable
- Valence electrons most reactive
Atomic weight
avg mass of all isotopes using mass of respective abundancies
Molecular weight
weight of a molecules different atoms summed
Ions
atoms that lose/gain valence shell electrons
- cations and anions
Polyatomic ions
ions composed of more than one atom
Nomenclature of anions/cations
ous or ic is more?
ate or ite is more?
Elements with more than one cation indicated by Roman numerals or suffixes -ic and -ous
ex. Fe2+ = Iron (II) = Ferrous ion
Fe3+ = Iron (III) = Ferric ion
Monatomic atoms use suffix -ide
ex. Hydride, oxide
Anions with oxygen = oxyanions
- hypo___ite (less oxygens)
- ___-ite
- ___-ate
- per___ate (more oxygens)
Carbonate = CO3^2-
Hydrogen carbonate = HCO3^2-
The Bohr Model (picture)
Energy levels, quantum numbers
n=1 is the ground state, for an electron to jump to a higher energy level it must absorb energy in the form of a photon of light (“excited”)
- High to low, electron emits a photon of light
- Energy is electromagnetic radiation (visible light, gamma rays)
Energy of a photon equation
E = hf
f = c/(λ)
E = hc/λ
h= planck’s constant (6.626 x 10e-34 J/Hz)
f=frequency
(λ)= wavelength
Measuring quanta (Rydberg formula)
When electron jumps energy levels, energy is emitted or absorbed in discrete amounts called quanta
- Atomic emission/absorption spectrum is unique to each element
change in E = hc/λ = R(1/ni^2 - 1/nf^2)
R= 2.18 E-18 J
h=plancks
n= energy level initial and final
Quantum numbers
shell, subshell, orbital, and momentum within orbital
Heisenberg uncertainty principle
exact position and momentum of an electron can’t be simultaneously measured
Pauli exclusion principle
no two electrons in an atom can have same 4 quantum numbers
Principle quantum number (n)
energy level
- higher # = higher energy
Angular momentum quantum # (l)(azimuthal)
subshell, specifies shape of orbital (s,p,d,f)
l=0=s, l=1=p, l=2=d, l=3=f
l = n, (n-1)
If n=1, l=1,0 (both s and p subshells)
Magnetic quantum # (Ml)
Specifies spatial orientation of orbital
-l to +l
Each orbital can only hold 2 electrons; s holds 2, p holds 6, d holds 10, f holds 14
Spin quantum # (Ms)
negative half or positive half spin (-1/2), (1/2)
Electron configuration (picture)
Aufbau principle: fill lower energy levels first
- Electrons always removed from subshell w/ highest electron # (n) first
Hunds rule
every orbital in subshell gets 1 electron before any get 2
** half filled and fully filled sub shells are most stable
Effective nuclear charge (Zeff)
Attractive force of positively charged nucleus on atoms valence electrons
- if Zeff is stronger, radius is smaller
Ionization energy
energy required to remove on valence electron from a neutral atom in the gaseous state
- 1st ionization energy is lower than the 2nd, removal reduces electrostatic repulsion and makes it harder to remove another (hardest to pull from more stable configs)
ATP
adenosine triphosphate, source of energy in a cell
- breaking off a phosphate group is energetically favored
- can be coupled w/ energetically unfavorable reactions to drive them forward
Two common e- carriers
NAD+ and FAD
- reduced forms are NADH and FADH2
Common redox reactions
Glucose and fatty acids are reduced biomolecules that are oxidized in energy producing pathways
A + B –> (A+) + (B-)
Polar covalent bond
Electrons distributed on more electronegative side
ex. H-Cl
H-bonding
ON/OF
Polarity of functional groups (picture)
hydrocarbons -> aldehydes/ketones -> amines -> alcohols -> carboxylic acids -> charged molecules
Polar func groups can be outweighed by larger non polar structures
*Charge outweighs non polar sterics
Protein polarity is used for
Enzymes, transmembrane proteins, and folding all use polarity
- active site on an enzyme is specific for its substrate, diff properties disrupt function
- protein folding primarily affected by tertiary structure, interactions b/w side chains of amino acids
Plasma membrane permeability
permeable to very small uncharged molecules and lipid soluble non polar molecules
Hormones
signaling molecules that travel through the circulatory system to induce various effects on their target tissues
- homeostasis and response to stimuli
- 2 types
Peptide hormones (what they’re made of, what they do)
Chains of amino acids, large and polar
- Can’t diffuse into cell, must interact via membrane receptors and secondary messengers (QUICK ONSET< SHORT LASTING)
Steroid hormones (what they’re made of, what they do)
derived from cholesterol, non polar
- Can diffuse into cell, interact with nuclear receptors that regulate gene transcription (LONG LASTING)
Histone modification
DNA is highly negative, histones act as a scaffolding to package DNA
- Noncovalent interactions (histones positive rich basic amino residues)
- Histones are modified by covalent additions of methyl, phosphate, and acetyl groups
ex. When acetyl group is added to lysine side group of a histone, removes positive charge which weakens interaction with DNA and creates space for transcription factors –> up regulates gene expression)
Metabolic pathways
Glycolysis, Gluconeogenesis, Citric Acid Cycle, beta-Oxidation
Glycolysis (what it does and reaction)
Cell to get energy out of glucose without using oxygen
- occurs in the cytoplasm
glucose + 2(NAD+) + 2ADP + 2pi –> 2 pyruvate + 2 ATP + 2NADH + 2H2O + 2H+
*understand what each does and is
Committed step of reaction
Steps that are energetically unfavorable tend to be highly regulated
Feedback
Early steps tend to be regulated as negative feedback; Final steps can be regulated to monitor end product concentration
Basic amino acid structure
Side chain (R), Carboxylic acid (COOH), Amine group (NH2), a-carbon
*side chain gives unique properties
*a-carbon usually a chiral center
-Amines and carboxylic acids act as backbones for polypeptide, side chains stick out to interact with environment

Chiral
Non-superimposable mirror images
Enantiomers (amino acids)
Can rotate plane polarized light clockwise or CCW
-R or S: based on structure (most aminos are S except for cysteine and glycine which are achiral)
-D or L: based on rotation of PPL (L for naturally occurring amino acids)
Non-polar amino acids (largest category)
Side chains either have no polar bonds or predominantly hydrophobic
- Aliphatic (straight chain) hydrocarbon side chains
Glycine, Alanine, Valine, Leucine, Isoleucine, Methionine, Proline, *Phenylalanine, *tyrosine, *Tryptophan
Glycine (Gly, G)
Simplest amino, H side chain, nonpolar
-achiral; doesn’t rotate plane polarized light
Alanine (Ala, A)
Methyl side chain (CH3)
- nonpolar
Valine (Val, V)
Isopropyl group, nonpolar
- Substitution in place of glutamic acid and hemoglobin causes sickle cell
Leucine (Leu, L)
Isobutyl group, nonpolar
Isoleucine (Ile, I)
TERTIARY carbon, nonpolar
Methionine (Met, M)
nonpolar, 1 of 2 aminos with a SULFUR atom (cysteine)
*C-S bond quite nonpolar
- Found in eggs and DNA methylation
- more inert than cysteine, sulfur is between two carbons
Proline (Pro, P)
AMIDE RING, nitrogen is part of side chain
- Gives ability to break up secondary structure of proteins by “proline kinks”
- Almost never find them in a-helices or B-pleated sheets (unless at the turn)
3 Aromatic Nonpolar Aminos (Benzene rings)
Phenylalanine, Tyrosine, Tryptophan
- electron delocalization
Phenylalanine (Phe, F)
single benzene ring side chain, non polar
- diet soda artificial sweetener
Tyrosine (Tyr, Y)
Benzene ring + OH group
- Amphipathic but more nonpolar due to bulky ring
Tryptophan (Trp, W)
TWO rings: Amide ring connected to benzene ring
- nonpolar
precursor to serotonin and melotonin
Polar but Uncharged Aminos
side chains have 1+ polar bond which shapes its behavior
- Serine, Threonine, Asparagine, Glutamine, Cysteine
Serine (Ser, S)
Alcohol side chain, relatively reactive
- polar but uncharged
- targeted by phosphorylation
- post-translational modification and signaling

Threonine (The, T)
Secondary hydroxyl group
-polar but uncharged
Asparagine (Asn, N)
Amide group (CONH2) - polar but uncharged
Glutamine (Gln, Q)
methyl then amide group (CH2CONH2)
- polar but uncharged
Cysteine (Cys, C)
SULFUR, thiol group (SH)
- sulfur is at end of chain
- not strongly polar but can participate in H-bonding
- 2 cysteine can form covalent disulfide bonds (contributes to proteins tertiary structure/3D shape)
Basic Amino Acids (positively charged)
Lysine, Arginine, Histidine
All have +1 charge, NH3+ side chain and amine group and COO- carboxyl

Lysine (Lys, K)
Protonated amine group, basic amino
- fairly reactive target for methylation, acetylation
Arginine (Arg, R)
3 amine groups, most basic amino
- Positive charge can be resonance stabilized
Histidine (His, H)
2 amines in one ring, basic
- Under physiological conditions its neutral (deprotonated)
Acidic Amino Acids
Functional group readily gives up H+ (negatively charged)
Aspartic acid, glutamic acid
- at physiological conditions, both have charge of -1
- two negative COO- groups and one NH3+

Aspartic acid (Asp, D)
COOH group
- Aspartate is deprotonated version
- Along with Phe, component of artificial sweetener aspartame

Glutamic acid (Glu, E)
Longer hydrocarbon chain before COOH group
- under physiological conditions, deprotonated forms dominant
- Glutamate is deprotonated version
- Important neurotransmitter
Atomic Theory
- All matter consists of indivisible atoms (except radioactive decay)
- Atoms of same element are identical
- Compounds = atoms of 2+ elements
- Chemical reactions are atoms recombining
Must know polyatomics
Nitrate, Nitrite, Carbonate, BiCarbonate, Perchlorate, Chlorate, Sulfate, Sulfite, Hydroxide, Chromate, Cyanide, Permanganate, Acetate
Intramolecular bonding (between atoms)
Covalent- similar E.N. values, share electrons
- unequal sharing creates polarity
- E.N. differences
Types of intermolecular forces
not bonding, between molecules, much weaker than intramolecular forces
- London dispersion
- Dipole-dipole
- H-bonds
- Ion-dipole
- Ionic
London dispersion
Weakest force can occur b/w any molecules, temporary dipoles arise by chance
*Larger molecules have stronger London forces
Dipole-dipole
Polar molecules partial charges
H-bonds
Stronger dipole-dipole bonds (more EN atoms)
Ion-dipole
Ions and molecules w/ dipole moment
Octet rule exceptions
8 electrons in valence shell for both bonding atoms except:
- Hydrogen only req 2 electrons
- Be: 4
- Boron: 6
- 3rd period and below elements can have expanded octet (phosphorus, sulfur)
Formal charge equation
= valence e’s - bonds - lone pairs
Molecules try to minimize formal charge
Synthesis/combination reactions
2+ reactants –> single product
ex. Haber process
N2 + 3H2 –> 2NH3
Decomposition reactions
single compound –> multiple products
- endothermic: energy must be invested to break chemical bonds
ex. H2CO3 –> H2O + CO2
Single displacement
One group replaces another
AB + C –> AC + B
**Often ionic compound, ion replaced by similar
- metal replaces metal, one ion more reactive than the other
Double displacement
AB + CD –> AD + BC
**Many pushed forward by producing insoluble precipitate (solid)
Neutralization
Acid + base –> H2O + salt
Acid contains H+ and base contains OH, can result in solution with neutral pH depending on concentrations
Combustion
Compound reacts (burns) in the presence of oxygen
- hydrocarbon + oxygen –> CO2 and water
- Highly exothermic, release heat/energy
- change in H < 0
Oxidation Reduction (redox)
OIL RIG
Characterized by electron transfer
- Oxidized compound gives up electrons, reduced compound gains them
- One of most prevalent reactions in the body
- Oxidation of glucose during cellular respiration, coupling of NADH oxidation and NAD+ reduction, citric acid cycle
Alkanes least oxidized (no bonds with oxygen), alcohols slightly more oxidized with one bond to oxygen, carboxylic acids most oxidized with 3 bonds to oxygen
Law of Conservation of Mass
Mass in an isolated system is neither created nor destroyed
Peptide bonds are
Bonds that join amino acids to form peptide chains
- N-terminus of one amino to c-terminus of another
- Releases OH of carboxyl group and H (H2O)
- Nucleophilic substitution: lone pair or amine attacks carbonyl carbon
Condensation/Dehydration reaction creates?
creates H2O (condensing two molecules into one)
What facilitates peptide bond formation and where?
TRNA in ribosomes
Peptide bond breaking = (type of rxn)
hydrolysis
- molecule of H2O adds to carbonyl group and kicks off amine group
Is peptide bond breaking favorable?
Energetically favorable but extremely slow under physiological conditions (good thing for body)
What enzyme catalyzes breakdown of peptide bonds?
Proteases destroy primary structure, also assisted by acidic conditions in stomach (stomach pH is 2 and still requires enzymes to break down proteins)
What makes peptide bonds stable under intracellular conditions?
Resonance, gives planar formation that disallows rotation around peptide bond
Protein primary structure
When does peptide become dipeptide
linear chain of aminos form backbone of protein, has DIRECTIONALITY
- proteins classified depending on length of chain
- peptide = <50 aminos (dipeptide, tripeptide)
Much harder to disrupt than higher level structures
- product of protein denaturation
How is protein size reported? Avg size of one amino?
Reported in molecular mass (kDa); 110 daltons
- 1 dalton = 1 amu = 1 g/mol
Protein primary structure directionality
New aminos added to carboxy terminus
Protein secondary structure (types)
First layer of protein folding, local regions/small sections
- Alpha helices
- Beta pleated sheets
** backbone interactions, no side chain interactions
- some aminos favor forming a-helices or b-pleated sheets, others known to disrupt secondary motifs
-many proteins have unique secondary structure
Alpha helices
Secondary protein structure (backbone interactions)
Common in DNA binding proteins, fits neatly into grooves of DNA helix; stabilized by H-bonds between residues 4 apart (amino to carboxylic group)
- also common in membrane spanning proteins
Beta pleated sheets
Secondary protein structure (backbone interactions)
Formed by beta strands, line up next to each other parallel or antiparallel
- implicated role in amyloidosis
- buildup of misfiled proteins, Parkinson’ and Alzheimers
- Proline introduces kinks in chains at turn of sheets
Tertiary protein structure
Determines fully folded functional state, 3D shape of polypeptide chain
** Side chain interactions
- Non-covalent, driven by polarity or charge
- Salt bridges (ionic bonds, basic and positive amino and acidic negative side chain bonded)
- Hydrophobic interactions (nonpolar molecules grouping together)
- Disulfide bonds (sulfur atoms of cysteine residues, forms via redox rxn; can be broken by reduction but stronger than ionic and dipole based interactions)
Organogenesis
First trimester of pregnancy, major organs develop, fetus continues to grow in 2nd and 3rd trimesters
Placenta
Fetus exchanges nutrients, gases, and waste products with mother
- Highly vascularized tissue, brings maternal and fetal circulation into close, but not direct, contact for diffusion of nutrients and oxygen from maternal to fetal blood vessels
- Also diffusion of metabolic waste from fetal to maternal blood vessels
Also secretes hormones
Fetal blood vessels
Umbilical arteries (carry deoxygenated blood away from fetal heart) and umbilical vein (carries oxygenated blood to fetal heart)
Arteries carry blood ___
Carry blood away
Veins carry blood ___
Towards the heart
Hemoglobin
Carrier protein responsible for transporting oxygen in the blood
Fetal hemoglobin
Especially high affinity for oxygen compared to adult hemoglobin
- can readily steal oxygen from maternal circulation
Placenta secretes hormones…
Human chorionic gonadotropin (hCG) (pregnancy tests test for this)
Later progesterone and estrogen to maintain pregnancy
Sexual differentiation
Default developmental pathway is female, precursor structure called Mullerian duct develops into uterus, cervix, and upper third of vagina
- Presence of sex determining region (SRY gene) on the Y chromosome halts this progression and reroute toward development of male sexual organs
- Y chromosome: much smaller and contains fewer genes, SRY is “main content”
SRY gene
Gene on Y chromosome, codes for transcription factor that causes testes to develop in males; prevents development of uterus and Fallopian tubes
Testes
Secrete androgens like testosterone, result in male fetus developing Wolffian duct which later forms male reproductive organs
Pregnancy lasts…
37 to 41 weeks, splits into 3 trimesters and culminates into labor and childbirth (parturition)

Oxytocin (cuddle hormone)
Exhibits rare example of positive feedback, stimulates uterine contractions during labor
- Contractions induce more oxytocin release from pituitary gland until childbirth
What fraction of people diagnosed with cancer in lifetime?
1/3
Tumor
Mass of tissue with abnormal cell proliferation, cells divide more than normal cell cyle
- most brain tumors are
Benign tumor
Tumor remains localized and contained in one area
- tumor doesnt invade basement membrane and spread to other tissues, a process known as metastasis
- can continue to undergo further mutation and become malignant
Can cause damage to tissue, press on nerves or blood vessels, and a benign brain tumor can be fatal
Malignant tumor
Invades through basement membrane and may spread to other tissues and organs
- In order to become malignant and develop into cancer, tumors cells must exhibit uncontrolled growth and gain ability to invade basement membrane and metastasize to other tissues
- form secondary tumors
- Get more aggressive with mutation that allow proliferation and rapid spread
- many cancer cells secrete growth factors and upregulate expression of growth factor receptors
- Also produce proteases that digest components of the extracellular matrix, providing an escape path through basement membrane
Cancer
Metastasis of a malignant (virulent or infectious) tumor
- cancer cells frequently secrete factors that promote angiogenesis, the formation of new blood vessels, which provide the highly metabolic tumor with an oxygen and nutrient supply
- In early stages of cancer, tumor antigens may be recognized by immune cells
- destruction of offending cells
- tumor cells can change how they express proteins on cell surface to avoid recognition
- mRNA, protein, miRNA becomes highly dysregulated compared to tissue of origin
Tumorigenesis
Formation of tumors, starts with one cell that is able to bypass normal cell cycle checkpoints and begin to divide abnormally
Can be caused by mutation in a gene that regulates mitosis and cell proliferation
- However, typically begins with an accumulation of mutations in critical genes that together allow a mutinous cell to divide when it shouldn’t, evading normal controls on cell division and growth
Tumor progression driven by process of natural selection, descendant daughter cells proliferate more rapidly, evade the immune system, thrive in anaerobic environment of tumor, and survive other checkpoints will be selected for and predominate in the tumor
De novo mutations
In dividing cells, mutations that arise spontaneously due to errors in DNA replication at a rate of about 1 error per 100,000 bp
- Proofreading enzymes catch and repair about 99%
- overall rate of 1 mutation/10 million base pairs
- 6 billion bp in a diploid cell = 600 mutations/1 diploid cell
Tissues that divide frequently
Epithelial cells in the skin, liver or digestive tract
- More likely to develop cancer
Most brain tumors are gliomas from supportive glial cells in the brain or metastases from primary tumors located elsewhere
Cells that divide infrequently
Neurons
Carcinogens
Cancer causing mutagenic agents
- chemicals, radiation (UV, ionizing radiation like X-rays and gamma rays)
- UV radiation known to produce pyrimidine dimers between adjacent bp than if uncorrected can cause lasting DNA damage –> lead to cancer
Cell can survive mutations that occur in noncoding region of DNA or silent mutations in protein encoding genes
- Mutations that occur in critical genes typically trigger DNA repair or apoptosis (cell death) at cell cycle checkpoints, prevent cell from proceeding w/ mitosis
-
However, if mutations present in genes that regulate cell cycle checkpoints, cell can escape reulatory mechanisms and continue to proliferate
- will continue to accumulate mutations that allow them to evade other regulatory processes –> positive feedback

Chemotherapy
Regimented use of chemical agents (essentially poisions) to treat cancer
- Challenge- specifically targeting cancer cells
- Interfering with cell division (anti-mitotic drugs) affect healthy cells as well with high cell division/cell turnover
- Gastrointestinal symptoms and hair loss
Tumors can also develop chemoresistance, and stop responding to treatments
- more than one drug necessary
Oncogenesis
Formation of cancer, characterized by highly dysregulated gene expression favoring synthesis of RNA and proteins that promote growth of the tumor
- Oncogenes and tumor suppressor genes
Oncogenes and tumor suppressor genes
- Oncogenes- mutant genes promoting abnormal cell growth leading to cancer
- exist as proto-oncogenes that give rise to oncogenes when over-expressed
- tend to emerge from genes that code for growth factors, growth factor receptors, transciption factors, protein kinases, and other signaling molecules
- also found in cancer causing viurses that either insert oncogenes directly or upregulate existing proto-oncogenes
- Tumor suppressor genes- genes protecting against abnormal cell growth whose impaired function can lead to cancer
- block cell cycle progression, respond appropriately to DNA damage, repair DNA damage, prevent changes to cell adhesion
- if tumor suppressor is down regulated or mutated, cell is less able to protect against cancer
ex. TP53 gene encodes p53 suppressor protein, “guardian of the genome” (initiates repair or apoptosis), mutation for p53 renders checkpoints useless (50% of human cancers detect this mutation)
ex. BRCA 1 and BRCA 2 genes, repair DNA damage, heritable mutations associated with breast cancer and ovarian cancer (mutations associated with 80% risk in developing breast cancer)
* Genetic screening recommended for those with family history with breast or ovarian cancer
Tumor viruses (don’t need to know for MCAT)
Hepatitis B and C viruses (liver cancer)
Papilloma viruses (cervical and anogenital viruses (relating to anus or genitals))
Epstein-Barr virus (causes Burkitt’s lymphoma and Nasopharyngeal carcinoma)
Isomers
Molecules sharing the same molecular formula but different structure
Stereochemistry
How molecules are arranged in space
- Along with charge interactions, explains why molecules behave the way they do
Structural/constiutional isomers
Different ways molecules can be arranged given a molecular formula
functional isomers= structural isomers with different functional groups
Tautomers- structural isomers that exist in equilibrium
- keto-enol tautomers, at room temp keto form is favored
- deprotonated enolate form is also important for some reactions
- also enamine and imines, replace oxygen with nitrogen
** resonance does not equal tautomers
- resonance represents single underlying structure while tautomers require breaking and reformation of bonds

Stereoisomers: conformational isomers
Single pattern of connectivity, different spatial configurations
- rotating around single bonds
- rotating around double bonds - cis and trans
- chiral centers with 4 different substituents
Visualizing steroisomers
Newman projections - carbon carbon bond extends into page
- eclipsed (unfavorable, torsional strain) formations (0 degrees of separation between bulky substituents)
- staggered (maximize separation between bulky substituents)
- anti conformation = 180 degrees of separation, most favorable
- Gauche effect = less favorable, 60 degrees of separation

Angle strain
Angle between single bonded carbon atoms deviates from 109.5 degrees
Torsional strain
Eclipsing substituents on neighboring atoms
Steric strain
Substituents (even hydrogen) getting in each others way
- to resolve, cyclohexane switches between chair (most stable, prefers), twist boat, and half boat
- substituents can either be axial or equatorial, each carbon has one axial one equatorial (one down and one up)
- bulkier substituent strain minimized by equatorial
- cis: two bulky substituents point in same direction
-
trans: bulky substituents point in opposite directions
- both are stable

Geometric isomerism
Different orientation of substituents around double bonds
- cis/trans and E/Z classification
- double bonds have fixed planar shape
Cis- identical substituents on same side of double bond
Trans- identical substituents on different sides of double bond
E/Z- doesnt require substituents to be identical
- Z isomers- two higher priority sustituents on same side (zame side)
- E isomers- two higher priority substituents on different side

Cahn-Ingold-Prelog Rules (priority rules)
Priority determined by atomic weight of the atoms, heavier = higher priority
- if same, look at amu of atoms attached
- multiple bonds higher priority than single bonds
Chirality
Describes asymmetry of molecules in 3D space
Chiral centers- atoms with 4 bonds to 4 distinct groups
- type of sterocenter: atom bonded to 3 unique groups
Chiral if mirror image is distinct and nonsuperimposable
-
enantiomers- same chemical formula, share physical and chemical properties
- receptors discriminate for enantiomers
Achiral- molecule has superimposable mirror image (align perfectly)

Absolute configuration around chiral center (nomenclature)
Uses atomic mass priority
- lowest priority substiuent is in back pointing away
- if not, rotate molecule around axis
- Arrow from 1 to 2 to 3
- R= clockwise
- S= counterclockwise

d/l Nomenclature
How molecule rotates plane polarized light
- enantiomers rotate PPL in opposite directions
- clockwise = d
- CCW = l
Experimentally determined, limited use
Racemic mixture = 0 degrees rotation
D/L nomenclature
Classify aminos and monosaccharides
- Orientation of hydroxyl or amine group at highest number chiral carbon (bottom of Fischer projection)
D- hydroxyl/amine on right side
L- hydroxyl/amine on left side
**Maximum efficiency when carbohydrates/aminos are in same configuration
**assume all carbohydrates are D isomers and aminos are L isomers

Enantiomeric excess
ee = observed opitcal rotation/specific optical rotation x 100
Number of possible stereoisomers of a chiral molecule
2n where n = number of chiral centers
If two steroisomers share opposite configuration at each chiral center, they’re enantiomers (nonsuperimposable mirror images)

Diastereomers
Molecules with multiple chiral centers that differ at some but not all

epimers- stereoisomers differing at just one chiral center (can also be diastereomers but not always)
Meso compounds
Contain internal plane of symmetry (achiral even with chiral centers)
Anomers
Cyclic sugar compounds with hydroxyl groups that differ in orientation at chiral carbon/carbon 1 (anomeric carbon)
Glucose has a-glucose and B-glucose
mutarotation- interconversion between a and b forms

Ketogenic diet
Eat low carbs and high fats, body enters “ketosis”, fat burning machine (rapid weight loss)
Carbohydrates
Essential macronutrient essential to generate cellular energy
- contain C, H, O, name derived from empirical formula Cm(H2O)n
- made up of monosaccharides (sugars) to form disaccharides, oligosaccharides + polysaccharides
- monosaccharides can take linear or cyclic form

Linear monosaccharides
Contain carbonyl (C=O) and at least one hydroxyl group attached to carbon backbone
- if carbonyl is an aldehyde group, making sugar an aldose
- if carbonyl is in middle of backbone, its aketone group and sugar is a ketose
Classified according to number of carbons in backbone
- triose, tetrose, pentose, hexoses, heptoses
Fischer projections
3D molecules represented in 2D
Horizontal lines are coming out of page, carbons numbered from top to bottom

Cyclic carbohydrates
Most 5 to 6 carbon sugars exist cyclically
- different anomers with different properties
- cyclize via nucleophilic addition where hydroxyl group on 4th or 5th carbon acts as nucleophile and attacks carbonyl carbon
Hexoses can form six membered or 5 membered rings (angle strain too high for any smaller ring)
- sugars in 5 membered rings are furanoses, 6 membered are pyranoses (glucose)
- allows easier nomenclature than IUPAC

Hemiacetal
Formed when aldehydes when alcohol attack carbonyl carbon

Hemiketal- the same except second R group instead of aldehyde H
Emotion
3 components: cognitive (what comes to mind when feeling emotion), physiological (emotions manifest physically), behavioral (way we behave when feeling emotion; variable)
Have been adaptive in evolutionary trajectory
- question is degree to cultural specificity
Universal emotions: same meaning no matter where someone grows up, hardwired to predictable facial expressions
- happiness: smiling, wrinkling brow
- sadness: corners of mouth lowered, inner side of brows raised
- surprise: opening ones eyes wide and mouth slightly, raising brows
- fear: also involves widening eyes/raising eyebrows, but w/ lips retracted toward ears
- anger: lowering eyebrows, pressing lips together, glaring
- disgust: wrinkling ones nose, lifting upper lip
- contempt: pulling corner of mouth upward
Limbic system
Where emotion is rooted in the brain
- grouping of structures in midbrain (vicinity of thalamus in medial part of temporal lobe)
- amygdala: processing emotional stimuli
- has neurons that project to hypothalamus, an important link between nervous and endocrine system; both play important role in translating between stimuli, concious perceptions, and physiological manifestation of emotion
- amygdala: processing emotional stimuli
- emotion, motivation, memory
Emotions Physiological Effect
Anxiety and fear associated with activation of sympathetic nervous system (autonomic, fight or flight mechanism)
- dilation of pupils, reduced parastalsis, increased conductivity of skin, less blood flow of muscles responsible for digestion, incr blood sugar
Blushing - embarrassment, sweating - nervousness
Theories of Emotion: James-Lange Theory (1800s)
developed w/o benefit of modern findings in neurology
Stimulus -> physiological arousal -> emotion
Physiology shapes pyschological perceptions
Incomplete theory of emotion; different people can have different emotional/physiological responses to stimuli
Theories of Emotion: Cannon-Bard (1920s)
developed w/o benefit of modern findings in neurology
Stimuli -> physiological response -> cognitive response (depending on context) -> emotion
J comes before S
Experiment- researchers injected subjects w/ either epinephrine (adrenaline) or placebo and told them they were getting a made up vitamin and told they would have different effects (some told they’d have sympathetic effects and others foot numbness, others told nothing)
- while waiting, stayed with researcher who acted euphoric or angry towards them
- subjects handled emotions appropriate to what they were told
Theories of Emotion: Schachter-Singer (1960s)
Stimulus -> emotional response and physiological response simultaneously and separately -> jointly lead to behavioral response
Theories of Emotion: Lazarus (1970s-90s)
Priveleges cognitive assessment of entire situation
stimuli -> cognitive appraisal -> physiological arousal and emotion
Stressors
- Cataclysimic events: external and broad scale
- Events in daily life, transitions
independent stressors: outside of our control
dependent stressors: impacted by our own behaviors, within our control
avoidance conflicts: avoid
approach conflicts: want to approach
- avoidance-avoidance conflict is two bad options
- double approach avoidance- each choice has pros and cons
Stress appraisal
Primary appraisal: process through which a person sees an event as a threat or stressor
Secondary appraisal: assessment of ability to deal with stressor
Distress
Eustress
Neustress
Distress: form of stress with a negative effect
Eustress: positive stress, brings out the best (ex. athlete playing in big game)
Neustress: neutral stress, no impact
General Adaptation Syndrome
How body responds to stress
- Alarm- sympathetic nervous system activated
- Resistance- mediated by cortisol, chronic stress response
- Exhaustion- body’s resource drained, increased susceptibility to fatigue and illness (cortisol drained)
Most well known negative impact of chronic stress is elevated blood sugar levels, increased risk of cardiovascular disease, impairment of immune system
- reduced fertility and greater risk for psychological conditions (like depression)
Big topic of study for socio-economic outcome
Learned helplessness
Repeated exposure to stressors that one is unable to change/avoid (eventually stop trying)
- potential links to psychiatric conditions like depression
Coping Strategies to Stress
Maladaptive: unhealthy strategies ex. substance abuse, verbal emotional and physical aggression, self harm
- conditions can shape peoples habits
Adaptive: healthy responses to stress ex. meditation and exercise
- context matters: exercise could be associated with eating disorders
Motivation
Underlying purpose for our actions
-
Biological motivators- hunger, thirst, sex drive
- addiction, obesity, compulsive behaviors
- Sociocultural motivators- varies between cultures
Intrinsic and Extrinsic motivation
Intrinsic: comes from inside yourself
- find a certain activity to be rewarding on our own terms no apparent reward
- self sustaining and resilient
Extrinsic: external factors drive behavior
- some other reward (money, prestige)
- vanishes when reward does
Instincts
Hard-wired, fixed behavioral patterns
In humans, a behavior not an urge that happens automatically regardless of cultural context ex. urination, defacation and not hunger or thirst
Homeostasis
How our bodies maintain themselves to maintain a stable internal environment
- Use of hormones to maintain physiological parameters like blood glucose levels, fluid and electrolyte concentrations
Drive
Urge to return some parameter to homeostasis
- Powerful motivators like hunger and thirst, sleepiness
Drive Theory: an excitatory state produced by a homeostatic disturbance
Drive reduction theory: motivation comes from a desire to return to homeostasis
Primary drives: basic, biologically grounded needs
- hunger, thirst, avoiding extreme heat or cold
Secondary drives: less basic needs
- recognition, social prestige, money (grey area)
Maslow’s Heirarchy of Needs (motivation)
Can’t focus on higher up needs until basic needs are satisfied

Psychological Arousal (motivation)
People are motivated to engage in actions that optimize psychological arousal
- don’t like to be bored or overwhelmed
Yerkes-Dodson Law: performance at various tasks is optimized by medium levels of arousal
Incentive Theory of Motivation
Reinforcers (motivation)
Expectancy-value Theory
Self-determination Theory
Opponent process Theory
- Incentive theory of motivation: humans respond rationally to external incentives
Primary reinforcers: rewards that correspond to basic physiological needs
Secondary reinforcers: psychologically complex concepts (recognition or appreciation)
- Expectancy-value theory: motivation is a reflection of the balance between expectancies(how successful we think we’ll be) and values(is task worthwhile)
-
Self determination theory: emphasis placed on intrinsic motivation
- people feel inherently motivated to engage in tasks that they are competent at performing
-
Opponent process theory: If a certain experience initially provokes an intense reaction, the opposite reaction tends to predominate
- ex. addiction
Attitude
Pyschological orientations that people have towards another person, activity, topic
- broad category, if we can direct our attention to something we can have an attitude about it
3 Components:
- Affective- feelings we have towards something or someone (emotional)
- Behavioral- how we act (shaped by affective and cognitive)
- Cognitive- underlying analytical perceptions
Effects of behavior on attitude:
Foot in the door technique
Induce compliance to a large technique by first getting someone to agree to a small request
Effects of behavior on attitude:
Role-playing
Simulating behavior can shape one’s attitudes
Effects of attitude on behavior:
Thomas theorem
If people define situtations as real, those situations have real consequences
Effects of attitude on behavior:
Cognitive dissonance theory
The discrepancy when a certain attitude or behavior is confronted with conflicting evidence
- People modify behaviors to match attitudes or vice versa
- ex. addictive/compulsive behaviors, anti-vaccine movement
Ways of relieving cognitive dissonance:
- acknowledge conflicting evidence, appeal to justifications, acknowledge risk but create hypothetical considerations or plans, downplay the risk, cast doubt or express skepticism
Elaboration-Likelihood Model (different ways of being persuaded)
Central route of processing: rational decisions based on advantages and disadvantages of choices
- Deeper thinking/processing, more stable outcomes
Peripheral route: superficial decisions based on gut reactions and surface level characteristics
- Less stable
Social Cognitive Theory (attitude and behavior)
Modeling desired attitudes and behaviors can be a strong method of changing attitudes
- establishment of social norms can also be very persuasive
Influencing Human Behavior
- Appeal to central or peripheral route processing
- Targeting message to appropriate group
- Appealing to social factors
- Persuasion can be resisted by using central route reasoning or encountering cognitive dissonance
- patterns of denial and minimization that result from cognitive dissonance
Classical Conditioning (paradigm)
Pavlov’s Dogs- dogs salivate in respone to smell of meat
- paired the smell of meat with a metronome, salivated in response to the metronome
- Smell of meat = unconditioned stimulus
- Salivating = unconditioned response
- Metronome at beginning = neutral stimulus
Acquisition= successful conditioning
After acquisitioning smell of meat to the metronome, salivating becomes conditioned response and metronome becomes conditioned stimulus
Extinction= eventually, without pairing, the conditioned response will go away (habituation, repeated stimuli elicit a diminished response over time)
- spontaneous recovery= conditioned response re-emerges without another conditioning process
-
stimulus generalization= stimuli similar to the conditioned stimuli may evoke the conditioned response
- discrimination= ability to distinguish similar stimuli
Dishabituation= intervening stimulus resensitizes person to original stimulus
Types of Historically Important Experiments:
- Those that discover a new fact or phenomenon
- Those that shed light onto previously unknown mechanisms underlying familiar behavior
- Pavlov’s dog experiment
Operant Conditioning (B.F. Skinner)
Reward (reinforcers)
reinforcment: anything that increases the frequency of a behavior
- positive stimulus (something is added) or negative stimulus (something is removed)
- positive or negative reinforcement
punishment: anything that decreases the frequency of a behavior
- positive stimulus(something added to punish) or negative stimulus (something taken away to punish)
- positive or negative punishment
Escape learning: learning a behavior to terminate an aversive stimulus (ex. turning off an alarm clock)
Avoidance learning: learning a behavior to prevent an aversive stimulus from occuring
Continuous reinforncement: provide reinforcement everytime behavior is performed; extremely effective but hard with limited resources
Partial reinforcement: reinforcement applied in some cases
- variable more effective than fixed
- ratios more effective than intervals
- variable ratio schedule is fastest for acquisition (casinos with slot machine)
Shaping: gradual approximation of a target behavior
Instinction is a concern similar to classical conditioning; instinctive drift

Behaviorism
B.F. Skinner, psychology studied through observable behavior rather than guessing internal states
Operant conditioning with classical conditioning
Use primary reinforcer (stimuli an animal is biologically programmed to respond to) and use classical conditioning to associate it with a neutral stimuli = conditioned/secondary stimulus
Latent learning
subconscious retention of information without reinforcement or motivation
Observational Learning
Learning can happen merely through observation
- Alfred Bandura (1961) children watch adults hit bobo dolls (bounce back up when hit) and hit them themselves
imitation is a subtype but people extrapolite observations to their own context
Can be a source of learning of what not to do
Mirror neurons- fire when someone is performing an action and also observing a similar action, contribute to observational learning
- also contribute to empathy, feeling someones emotions from their perspective
How memory is processed in our mind (2)
Encoding- store and perform cognitive processes on
Can process environmental input automatically or deliberately
- Conscious and unconscious techniques affect the ease of encoding
-
Priming: effect of context on our ability to perceive stimuli
- positive and negative
- Chunking: complex stimulus broken down into smaller easier to encode components
- Mnemonics
- Method of loci: mentally mapping info onto an imaged space (like a house w different rooms)
Pyschological arousal restricts our focus of attention
Sensory memory
Sensory memory- instantaneous, at any given time, temporarily stored and will decay in matter of seconds without rehearsal/reinforcement
Long-term memory
Long-term memory- hours to years, storage not limited
- semantic (explicit) memory- memory of specific pieces of information (ex. trivia)
- procedural (implicit) memory- memory of how to do something (ex. riding a bike)
-
episodic memory- memory of experiences
-
misinformation effect (memory retrieval): information we subsequently obtain can affect how we remember the original event
- can cause witnesses in a trial to be biases; once they learn someone is a criminal they see them in a certain light during past memories
-
misinformation effect (memory retrieval): information we subsequently obtain can affect how we remember the original event
Short term/working memory
Short term- tens of seconds to minutes, limited capacity
Working memory- cognitive and attentional processes used for short term memory
visuospatial sketchpad: a buffer that holds on to visual and spatial memory as it’s processed by working memory
Flashbulb memory
Many of us have experienced having extrememly vivid memory of moment in our lives (usually emotion)
Eidetic (photographic) memory
Ability to remember a stimulus in great detail after a relatively short exposure
Iconic memory
How a highly detailed visual image can remain in our perceptin after the stimulus itself is removed
Prospective memory
Memory about plans to do something in the future
Memory storage
spreading activation-
schemas-
source monitoring errors-
Stored in semantic networks- heirarchical storage, linear top down approach; doesnt capture everything
- also have to account for metaphorical or emotional associations
- ex. rocking chair stored chair category in furniture category
-
spreading activation- when a concept is brought to mind, spreads to adjacent nodes of network
- schemas- ways in whcih we organize our knowledge about the world
- source monitoring errors- memory or knowledge is correct but misattribute its source
Memory retrieval
Process of calling upon memories and stored knowledge
- distinction between recall (active) vs. recognition (passive)(easier than recall, req shallower knowledge)
- semantic activation- can more quickly retrieve adjacent concepts
Several factors can help or hinder recall of items:
- Serial position effect: extreme ends easier to recall
- Primacy effect- people more likely to recall items at the beginning of a list than in the middle
- Recency effect- items at the end of a list are easier to recall than the middle
- Spacing effect: recall more effective when learning process is spaced out
- Dual coding effect: studying multiple modalities is more effect than one
Emotion and memory retrieval
Emotions can also effect memory retrieval, emotionally intense memories more likely to be stored
Being in a certain mood might favor recollection of similar emotional overtone
State-dependent effect- certain mood might promote the recall of memories that were encoded when you were in a similar mood
- also applies to states of consciousness (drugs)
- being in the same physical setting where a memory was encoded and stored can promote its recall
Reproductive memory: we encode info and reproduce it as needed; insufficient oversimplification
- In reality, memory is reconstructive: we build memories based on our perceptions of ourselves and others, context of events, etc.
False memories: (often not deliberate) memories reconstructed and not recorded
Memory loss
Inevitable; relearning is faster than learning the first time, each successive round more successful
- Ebbinghaus forgetting curve: repeated rounds of learning slows down the forgetting process and consolidates more information into long-term memory
Interference
- Proactive interference: old memories inhibit the consolidation/retrieval of new ones
- Retroactive interference: new memories/knowledge interfere with older memories
Amnesia: losing memories of entire experiences, periods of time and/or information
- retrograde: inability to remember previous events
- anterograde: the inability to form new memories
-
Alzheimer’s disease: majority of long term dementia cases
- characteristics: neurofibrillary tangles involving tau proteins and plaques composed of beta-amyloid proteins
- forgetfulness and short term memory loss, progresses to more severe anterograde and retrograde , cognitive deficits, difficulties thinking, speaking, and emotional disturbances
- no known cure, no established preventive measures
-
Korsakoff’s syndrome: causes anterograde and retrograde amnesia
- confabulation: creating elaborate fictional stories
- caused by a deficiency of thiamine (Vitamin B1)
- severe alcoholics and eating disorders
- preventable through proper nutrition
Aging does reduce fluid intelligence and speed of acquiring knowledge, but does not cause loss of previously acquired knowledge and crystallized intelligence

Biology of memory
Synaptic connections:
- formation
- strengthening
- pruning or loss
- important stage of early childhood development
- autism
- important stage of early childhood development
Nueroplasticity- ability of brain to rewire itself in response to learning new information or to compensate for disease or injury
- contributes to lifelong learning
Long term potentiation- strengthening, formation of synaptic connections
Solids
Fixed shape and volume, particles don’t flow or move past each other
-
amorphous- no order to particles, not quite as rigid
- glass, gels, polymers like rubbers and plastics
-
crystalline- highly ordered, repeating pattern
- table salt
- 4 types
- Ionic- made up of ionic compounds
- Molecular- molecules held together by non-ionic molecular forces
- ice
- Covalent network- covalent bonds
- diamonds with carbon atoms
- Metallic solids- metallic atoms with metallic bonds
- delocalized valence electrons give conductive properties
Liquids
No fixed shape, hard to compress, flow readily
Viscosity- resistance of liquid to flow
Surface tension- amount of energy needed to increase surface area of a liquid
- tension created at liquid surface by intermolecular attractions
- stronger than intermolecular attractions with surroundings
- Cohesive forces- attractive forces between same type of molecules
-
Adhesive forces- attractive forces between different types of molecules
- capillary action- movement of a liquid up sides of tube against gravity
Gases
Flow and have no fixed shape but readily compressible/expandable
- Particles free moving and spaced apart, little intermolecular interactions
- move randomly
- Pressure- amount of force particles exert on surroundings
- Solid transitions to liquid
- Liquid becomes gas
- Gas becomes liquid
- Liquid to solid
- Solid becomes gas
- Gas becomes solid
- Melting/fusion
- Vaporization
- Condensation
- Freezing
- Sublimation
- Deposition
Gibbs free energy (G)
∆G > 0 = nonspontaneous
∆G < 0 = spontaneous
- ∆G= ∆H - T(∆S)
- H = enthalpy; energy (like heat)
- increases is thermodynamically unfavorable, ∆G more positive
- H = enthalpy; energy (like heat)
- S = entropy; randomness, highest in gases
- energetically favorable, contributes to more negative ∆G (more spontaneous)
Enthalpy (∆H)
H = E + PV
E= internal energy

Q = mc∆T
How much temperature changes from addition of heat
Q= heat added (kJ)
m = mass (kg)
c = specific heat capacity (kJ/kg x K)
∆T = temp in Kelvin
Specific heat capacity of water is higher than of ice, liquid water can absorb more heat
Heating curve
For heating curves, temp increases until reaches value the bonds become broken and thats where phase change occurs
∆Hf = enthalpy of fusion = how much heat is needed to melt one mole of substance (kJ/mol) = Q/m (kJ/kg)
334 kJ/kg for water (energy required to melt 1 kg of ice)
∆Hvap= enthalpy of vaporizationm= Q/m
If we’re melting a block of ice into gas, have to conside q=mc∆T + ∆Hvap + ∆Hf

Phase Diagram
- Pressure (atm) on y axis
- Temp (K) on x axis
Phases in equilibrium along boundary lines
triple point- all three phases in equilibrium
critical point- beyond which, liquid and gas phases become indistinguishable
- beyond critical point, liquid/gas is super critical fluid

Alcohols (naming)
Organic compounds that contain hydroxyl (OH) group
- suffix -ol (ex. 2-pentanol, if OH is on carbon 1 its number is ommited, like ethanol)
- diol has two carbon substituents
- common naming adds -yl, ex. propyl alcohol
- when OH isn’t highest priority, hydroxy- prefix
Alcohol properties
Melting and boiling points are high due to H-bonding, increases with additional OH’s
- Alcohols are weakly acidic (pKa from 15-17, weaker than water)
- can be made stronger by adding electron accepting substituents (like adding a chlorine) and weaker with electron donating
- ***anything that pulls electrons from oxygen in OH group makes acid stronger, easier for H to leave
- Adding alkyl groups makes alcohol more basic
- *** all acids and bases have this ability but alcohols have wide range of pKa values

Conjugate base of an alcohol (deprotonated)
Alkoxide- strong base (***weaker the acid = stronger the base)
Alcohol as functional group (reactions)
Can react with oxidant to form ketone or aldehyde, acid/base reaction to form ether; can also form alkenes, thiols. epoxides and halohydrins
- Makes alcohols essential for pharmaceuticals, organic industrial materials
MCAT televant reactions:
-
Oxidation-**increase in number of bonds to electronegative element or decrease in bonds to H
- energy released by spontaneous redox reaction is converted to electrical energy
- Reduction is the opposite, increase in bonds to H, but alcohols undergo oxidation

Alcohol oxidation
Weak oxidizing agent (common one is PCC) converts alcohol to carbonyl
Stronger oxidizing agent converts alcohol to carboxylic acid (sodium dichromate, potassium dichromate, chromium trioxide)
- Only one step away from carbon dioxide (most oxidized form of carbon)
- secondary alcohols can only become ketons, tertiary can’t be oxidized
Metal + oxygen atoms = oxidizing agent

Alcohol protection in reactions
Want to react something other than alcohol in a reaction, must protect it (make it unreactive) with a protecting group: Silyl ethers, mesylates, tosylates
- silyl ethers: use silyl chloride and alcohol; to get alcohol back, treat substrate with fluoride ion to break Si-O bond
- mesylate: react alcohol with methanesulfonyl chloride
- also make alcohol into better leaving group without adding acid
- tosylate: react alcohol with toluenesulfonyl chloride
- also make alcohol into better leaving group without adding acid
Alcohols can also be used to protect other functional groups (carbonyls)
Phenols
Hydroxyl group added to aromatic benzene ring
- more complex phenols can be created with additional substituents
Especially acidic due to aromaticity (acid strength = stability of conj base)
- without H on OH group, resonance throughout ring
- if add electron withdrawing substituents, can lower pKa enough to act as acid
Nomenclature
- ortho(adjacent), meta (one carbon separation), and para (two carbon separation) describe orientation of two substituents on ring relative to each other

Phenol oxidation/Quinone
Hydroquinone (p-benzenediol) can be oxidized to form Quinone (becomes nonaromatic)
Quinones- electron acceptors that participate in biochemical reactions
- Ubiquinone (Coenzyme Q): liquid soluble electron carrier that hangs out in inner mitochondrial membrane to facilitate electron flow through complexes I, II, and III of ETC
- Can carry one or two electrons
- when carrying one, one carbonyl group reduced to an alcohol (Ubisemiquinone)
- when carrying two, both carbonyls reduced and called ubiquinol

Conjugation
have alternating single and multiple (here, double) bonds. This alternation allows for the overlap of p orbitals and the delocalization of electron density.
Protic
solvent that has a hydrogen atom bound to an oxygen (as in a hydroxyl group), a nitrogen (as in an amine group), or fluoride (as in hydrogen fluoride). … The molecules of such solvents readily donate protons (H+) to solutes, often via hydrogen bonding.
Water is the most common protic solvent
Pyruvate
Pyruvate: simplest alpha-keto acid (part ketone, part carboxylic acid)
- “2-oxopropanoic acid”
Carbonyl a-hydrogen (ketones and aldehydes)
The hydrogens on an alpha carbon, which are known as alpha-hydrogens, are weakly acidic and can be removed by a strong base.
- negative charge left behind when H is removed is stabilized by resonance (stabilized conj base raises acidity)
- negative charge shifted to Oxygen (happier on more electronegative atom)
- ***= ENOLATE; deprotonated form of enol
- Not the same thing as keto-enol tautomerism, which doesn’t involve deprotonation
- negative charge shifted to Oxygen (happier on more electronegative atom)
When the negative charge from deprotonation is on the alpha carbon and not oxygen, just as important for reactions
alpha carbon- any carbon adjacent to carbonyl carbon
Enol and Enolate
enol- combines alkene group (“en”) and hydroxyl group (“ol”)
When talking about aldehydes and ketones, also talking about biologically relevant molecules like
Pyruvate (major product of glycolysis), pyruvic acid
Ketones
Carbonyl bonded to two carbons
IUPAC suffix “-one”, carbonyl assigned lowest possible number if highest priority
- prefix “keto-“ or “oxo-“ for carbonyl
- common names-
- “acetone” simplest ketone, two methyls; common household paint thinner/nail varnish remover
Ketones can form hydrogen bonds, but they can only act as the acceptor (accepting the hydrogen) and not the donor. Ketones accept a hydrogen bond via the carbonyl oxygen

Aldehydes
Carbonyl bonded to a carbon and a hydrogen
IUPAC suffix “-al” and prefix
- if attached to a ring, may use suffix carbaldehyde
- ex. cyclopentanecarbaldehyde
Aldehyde and Ketone physical and chemical properties
Carbonyl double bond is highly polar = polar aprotic; capable of dipole-dipole interactions with other molecules but not hydrogen bond donors
- makes aldehydes and ketones ideal solvents for organic reactions; specifically SN2 reactions
- can dissolve polar reagents but not strong enough nucelophiles to interfere with reaction
Higher melting and boiling points than alkanes of similar size due to polarity; not as high as alcohols or carboxylic acids
*ketones less acidic than aldehydes due to extra electron donating group, tougher to lose alpha hydrogen
beta-dicarbonyl compounds- two carbonyls connected to alpha carbon, tend to be considerably more acidic due to both pulling electrons from a-carbon
Aldehyde and ketone reactions
Oxidation of glucose during cellular respiration, coupling of NADH oxidation and NAD+ reduction, citric acid cycle; At the heart of these reactions:
- glucose = aldehyde
- oxaloacetate and pyruvate = ketoacids
Aldehydes and ketones can function as both nucleophiles and electrophiles
- two reaction sites: carbonyl carbon = electrophile (partial positive) and alpha carbon = nucleophile (negative once hydrogen is removed)
- depending on if neutral or deprotonated, can tell how they’ll function in reaction
- also lookout for other components of reaction environment, like a strong base that could convert aldehyde/ketone
Aldehydes carbonyl carbon more reactive than ketones due to steric hindrance, carbonyl carbon in ketones harder to access
Oxidation of aldehydes/ketones
Oxidation of aldehydes to carboxylic acids:
- requires strong oxidizing agent (KMnO4)(K2Cr2O7)(Na2CrO4)(CrO3)(Jones reagent)
- can’t use mild oxidant PCC which creates aldehydes/ketones from alcohol
Ketones can’t be further oxidized to carboxylic acids due carbonyl carbon having no bonds to hydrogen; would require breaking carbon-carbon bond, goes beyond ability of even strong oxidizing agents
Reduction of aldehydes/ketones - nucleophilic addition
Aldehydes and ketones can be reduced to alcohols using hydride based reducing agents
- NaBH4, LiAlH4
Aldehydes/ketones also undergo nucleophilic addition reactions
- carbonyl oxygen gains a hydrogen to become (OH),
- nucleophilic attack by H2O breaks double bond and adds water
- newly added water is deprotonated, resulting in two (OH) groups
- Product is a geminal diol;
Same reaction with alcohol produces hemiacetal or hemiketal
- However, alcohol can continue to react and form acetal/ketal
Last addition reaction is with hydrogen cyanide, forms cyanohydrin
Reduction of aldehydes and ketones - nucleophilic substitution
Imine formation: nucleophile is an amine and Nitrogen from amin replaces carbonyl oxygen
- carbon to nitrogen double bond

Nucelophilic addition
Begin with nucleophilic attack, but no leaving group
- Oxygen protonated
- nucleophilic attack
- deprotonation
Common examples of nucleophiles: water, alcohols, hydrogen cyanide
- all have a spare electron pair to donate

Hemiacetal and hemiketal / acetal and ketal
Contain R group, OR group, OH group; hemiacetals have H group as well and hemiketals have second R group instead
Nucleophilic substitution of an alcohol to knock of hydroxyl groups and become acetal/ketal groups

Substrate
the substance on which an enzyme acts
or
an underlying substance or layer; the surface or material on or from which an organism lives, grows, or obtains its nourishment
Deprotonated aldehydes and ketones reactions
Alpha carbon functions as nucleophile,
ex. Aldol condensation: nucleophilic enolate of aldehyde or ketone attacks electrophilic carbonyl of another
Carboxylic acids nomenclature
IUPAC: “-oic acid”, highest priority of any functional group
Common names:
- acetic acid = ethanoic acid = vinegar
- formic acid = methanoic acid
- COOH w/ cyclic compound = “-carboxylic acid” suffix
- ex. cyclohexanecarboxylic acid
- Two = “-dioic acid”
- butanedioc acid = succinate; important substrate in aerobic metabolism
Carboxylic acid physical properties
Readily form hydrogen bonds which are stronger than alcohols
- Result in very strong intermolecular forces, high melting/boiling points
- Fairly acidic, hydroxyl group has pKa of 4-5
- lower with electron withdrawing groups to stabilize conjugate base
- **resonance stablized when OH is deprotonated, adds to acidity
- Inductive effect by electron withdrawing groups increase acidity
- diminishes w/ distance from COOH
- alkyl groups have opposite effect; electron donating
- Like aldehydes and ketones, a-hydrogen is also weakly acidic
- has renonance and creates enolates
Acids are stronger when conjugate base is more stable because
Inductive effect
If an conjugate base is very stable and favors being in its base form, then it’s acid form is more willing to give up its proton
Ranking compounds by acidity
- Functional group acidity
- Secondary characteristics: inductive groups and electron withdrawing groups
Carboxylic acid biological reactions
Saponification: triglyceride + strong base (such as NaOH), TGC esters bonds are broken by nucleophilic attack
- forms carboxylate anions at the end of hydrocarbon chain
- anion forms salt with cation left behind by base (in this case Na)
- used industrially to form soaps
Redox reactions:
- Reduced to alcohols with strong reducing agents(LiAlH3)
- Reducing to aldehydes requires medium reducing agent (DIBAL-H) in equimolar ratio
Decarboxylation: carboxyl group lost as molecule of CO2
- substrate usually 1,3-carboxylic acid
- favored at high temp and upregulated by decarboxylase enzymes
- Conversion of pyruvate to acetyl-CoA by pyruvate dehydrogenase complex for aerobic metabolism
- * also occurs in two reactions of citric acid cycle
- responsible for conversion of THCA to THC
Highly electrophilic carbonyl carbon allows for variety of nucleophilic substitution reactions, (OH) is good leaving group and replaced by nucleophile
- ammonia/amine creates amide
- esters formed by alcoholic nucleophile = FISCHER esterification
- acid anhydrides created by combining two carboxylic acids
Fatty acids
Carboxylic functional groups attached to nonpolar hydrocarbon chain
Hell-Volhard-Zelinsky Halogenation
Halogen added to carboxylic acid
Unlike other carboxylic acid reactions, uses alpha carbon
Bromination example:
- Phosphorus tribromide and diatomic bromine
- Bromine replaces hydroxyl group = acyl halide
- Keto-enol tautomerism yields enol version which reacts with diatomic bromine, bromine added to alpha carbon
- Carboxylic acid reformed with bromine on alpha carbon

Carboxylic acid derivatives
Esters, amides, acid anydrides
- derived by using appropriate nucleophile
- common in nature and industrialization
- amids make up peptide bonds in aminos and proteins
- low molecular weight esters common in fragrance industry, also responsible for pleasant aromas in fruits/oils
- triglycerides are esters of glycerols and fatty acids
- acid anhydrides used industrially to prepare acetate esters used for photography film and eyeglass frame
Derivatives closely reltaed and can be interconverted, ease of conversion depends on reactivity (determined by stability of leaving group and electrophilicity of carbonyl carbon; also have to consider steric hindrance)
- Carboxylates least reactive< amides< esters< carboxylic acids< esters< anyhydrides< acyl halides
- **can convert from less stable to more stable but not vice versa

Amides (carboxylic acid derivative)
amides- amine instead of OH in COOH group
- primary, secondary, or tertiary depending on type of amine used to produce them
- suffix “-amide”; if using secondary or tertiary amide, substituents on nitrogen atom identified with “N”
- ex. N-methyl-propanamide
More hydrogen substituents on Nitrogen leads to more H-bonding
- Means higher melting and boiling points
- More alkyl groups bonded to nitrogen means less H-bonding, lower melting/boiling points
Intermolecular forces weaker than alcohols/carboxylic acids
Weak bases, inert to acid base reactions because 1. carbonyl pulls electrons away from nitrogen and 2. resonance between them stabilizes the structure = less reactive
- carbonyl carbon is still electrophilic, allows some nucleophilic subs

Lactams
lactams- cyclic amides
- alpha = alpha carbon closes ring; beta = beta carbon closes ring, gamma and delta
- **beta: many drugs including broad spectrum antibiotics like peniccilin
- four membered ring, experience high ring strain
- **beta: many drugs including broad spectrum antibiotics like peniccilin

Esters (carboxylic acid derivative)
Can’t hydrogen bond = usually rather volatile; no acid base chemistry
Prone to acid/base catalyzed hydrolysis
IUPAC- two alkyl groups must be differentiated, one is bound to carbonyl group;
- “-oate” suffix given to carbonyl chain
- esterifying group (other chain) = “-yl”
- ex. ethyl hexanoate
Lactones
Cylcic esters, also use beta, gamma, and delta (depending on which carbon closes the ring)
Acid anhydrides (Carboxylic acid derivative)
Two carboxylic acids stuck together through condensation reaction
symmetric= replace “acid” in carboxylic acid with anhydride (ex. acetic anhydride)
asymmetric= name chains in alphabetic order (ex. butanoic ethanoic anyhydride)

Acyl halides (carboxylic acid derivative)
Reacting carboxylic acid with halogenated reagent
- can’t form hydrogen bonds, low boiling point
- however, extremely reactive
- halides excellent leaving groups
Carboxylate
Carboxylic acid anion
- resonance stabilized, unlikely to form good leaving group
Transesterification
Ester reacts with alcohol (has to be different from alcohol used to form the ester)
- new alcohol replaces esterifying group, results in new ester and new alcohol

Acid catalyzed amide hydrolysis
Molecule of water adds across amid bond, generating an amine and a carboxylic acid
- through this process that peptide bonds are broken in proteolysis
Enzymes called proteases/peptidases catalyze reaction, often specific between amino acids

life on earth began 3.8 b.y.a
Earth atmosphere had no oxygen for 1.8 b.y.
Many organisms don’t require oxygen, and our oxygen requiring metabolic pathways use anaerobic pathways
Glycolysis (aerobic vs. anaerobic cells)
Metabolic process common to all cells on earth; obtains energy from glucose regardless if oxygen is present. Doesn’t provide that much energy
- in cells that can use oxygen, other metabolic processes provide most of cell’s energy needs; glycolysis sufficient for simple anaerobic cells
In aerobic cells, glycolysis provides starting point for glucose breakdown and can serve as energy in conditions insufficient oxygen is present
Where does glycolysis occur?
Cytosol of cell
3 things to account for in glycolysis
-
One molecule of glucose –> 2 pyruvate (3-carbon alpha-keto acid)
- pyruvate has two carbonyls, glucose 5 hydroxyl groups == redox reactions
- 6 carbon glucose broken down into two 3 carbon molecules
-
Two NAD+ + 2H+ –> 2 NADH
- electron carriers which store energy
-
two ADP + 2 Pi –> 2 ATP (for every one glucose molecule)
- adding inorganic phosphate group to ADP
What pathways is pyruvate involved in?
- Citric acid cycle (aerobic respiration)
- Lactate fermentation (anaerobic respiration)
- Gluconeogenesis (during high ATP/ADP ratio)
- Fatty acid synthesis (energy storage)
Isomerase (enzyme)
Converts between two isomers
ex. glucose 6-phosphate isomerase converts between glucose and fructose (structural isomers)
Glycolysis number of steps and subdivisions
10 steps: energy investment phase first (5 steps) and energy payoff phase second (also 5 steps)
energy investment: cell spends 2 ATP to power several energetically unfavorable reactions
- glucose enters cell through glucose transporters (so it can’t escape if extracellular glucose gets too low)
energy payoff phase: 4 ADP to 4 ATP (gains more than spent), gain of 2 ATP per glucose molecule
Energy investment steps of glucose
- glucose enters cell through glucose transporters and enxyme hexokinase adds phosphate group = 6GP
- costs an ATP, traps glucose in cell (puts -2 charge on glucose, making it polar; also reduces glucose conc in cell, allows cell to pull in more glucose)
- Enzyme glucose 6-phosphate isomerase converts G6P to F6P (fructose 6-phosphate)
- name of enzyme tells us whats happening
- F6P converted to F1,6BP (fructose-1,6-biphosphate) by phosphofructokinase-1
- adds second phosphate group to substrate, another energy investment step
- ***most important step of glycolysis, no turning back point
- committed, rate-limiting step
- **highly regulated
- F1,6BP cleaved into G3P and DHAP (glyceraldehyde 3-phosphate and dihydroxyacetone phosphate)
- catalyzed by aldolase
- Converts DHAP to another G3P catalyzed by triosephosphate isomerase
- want to have two identical molecules for next steps
Added two phosphate groups and broke molecule in half to end up with 2 G3P –> ready for energy payoff phase
Energy payoff steps of glycolysis (starts with step 6)
*** Each step happening twice, one for each molecule of G3P (twice for each molecule of glucose)
-
G3P to 1,3-biphosphoglycerate (1,3PG) catalyzed by GADPH (G3P dehydrogenase) (redox reaction)
- creates a NADH from NAD+ and adds another phosphate
- Doesn’t require ATP because NAD+ production highly exergonic, which enzyme uses to add inorganic phosphate (substrate-level phosphorylation)
-
1,3PG to 3-phosphoglycerate (3PG) by phosphoglycerate kinase (PGK)
- one phosphate group pulled off to generate an ATP
- regulated step
- Phosphogylcerate mutase converts 3PG to 2PG (phosphate group moved over)
- Enolase turns 2PG to PEP (phosphoenolpyruvate)
- enzyme pyruvate kinase converts PEP to pyruvate, removes remaining phosphate group making another ATP
- regulated
2 molecules of G3P produce 1 pyruvate each, 2 ATP each, and 1 NADH
Used two ATP, net gain two ATP
Substrate-level phosphorylation
What can we do with products of glycolysis?
2 ATP, 2 NADH, and 2 pyruvate molecules
2 molecules of ATP can be used for energy
If cell can use aerobic respiration, NADH to electron transport chain to produce even more ATP
- pyruvate undergoes further modifications for citric acid cycle to make more ATP
In an anaerobic cell or under anaerobic conditions, need to regenerate NAD+ to keep glycolysis cycle going
- pyruvate and NADH undergo fermentation to do so
Why glucose need to be regulated?
If already have plenty of energy, burns glucose that can be stored and used when you need energy more.
also, cell would use up all NAD+, then get stuck in step 6 of glycolysis when it is required
- unable to convert G3P into 1,3PG
- why cells need electron transport chain or fermentation
Glycolysis is upregulated when cell needs ATP, and downregulated when cell has enough
In what type of cells is glycolysis strongly upregulated?
Cancer cells
How does the cell sense energy balance? (for glycolysis)
cell senses relative concentrations of ATP compared to ADP and AMP (byproducts of use of ATP for energy)
- low ADP and AMP compared to ATP means cell has enough energy
- high ADP and AMP and low ATP means cell is low on energy
High citrate and high NADH levels also signal cell doesn’t need energy through glycolysis
- citrate important intermediary of CAC and NADH product of CAC and glycolysis
- indicators cell has enough materials to make ATP
***end products inibiting what made them = negative feedback regulation
What hormones regulate glycolysis
Hormones insulin and glucagon
-
insulin upregulates glycolysis
- Insulin inhibits fructose 2,6-bisphosphatase and activates PFK-2, increasing fructose 2,6-bisphosphate which activates PFK-1 and stimulates glycolysis (committed step)
- insulin levels are high when blood sugar levels are high, want to be able to break down glucose and harness its energy
- Insulin inhibits fructose 2,6-bisphosphatase and activates PFK-2, increasing fructose 2,6-bisphosphate which activates PFK-1 and stimulates glycolysis (committed step)
-
glucagon downregulates it
- Glucagon activates fructose 2,6-bisphosphatase and inhibits PFK-2 (two components of bifunctional enzyme), reducing fructose 2,6-bisphosphate which downregulates PFK-1 preventing glycolysis (committed step)
- Makes sense because glucagon levels high when blood sugar levels are low, don’t want to use up that glucose
- want to liberate it into bloodstream for other cells to use
- Makes sense because glucagon levels high when blood sugar levels are low, don’t want to use up that glucose
- Glucagon activates fructose 2,6-bisphosphatase and inhibits PFK-2 (two components of bifunctional enzyme), reducing fructose 2,6-bisphosphate which downregulates PFK-1 preventing glycolysis (committed step)
One of insulins job is to get glucose into the cell
One of glucagons job is to get liver cells to produce glucose to push out into the bloodstream (gluconeogenesis)
1st regulatory step of glycolysis
- First step of glycolysis when hexokinase turns glucose into glucose 6-phosphate
- Prevents glucose from leaving the cell, however G6P is not committed yet (can enter glycogenesis and pentose phosphate pathway)
- G6P inhibits hexokinase, therefore prevents cell from making too much of itself
Liver and pancreatic cells contain special version of hexokinase called glucokinase, which has a lower affinity for glucose and isn’t regulated by G6P
- Allows liver and pancreatic cells to respond to amount of glucose in environment rather than demand for G6P and ATP in the cell
- Important because liver and pancreas have system wide functions in the body
What does liver do
Stores and releases glucose as glycogen for other body tissues
- liver cells needs to store and absorb more glucose than needed for their metabolic needs
2nd regulatory point in glycolysis
Committed step: 3rd step when phosphofructokinase-1 (PFK-1) creates fructose 1,6-biphosphate from F6P
Enzyme PFK-1 is downregulated by high levels of ATP and citrate, which indicate cell has enough energy
- upregulated when cell has too much ADP
Also regulated at organism wide level by insulin and glucagon:
- PFK-1 allosterically regulated by fructose 2,6-phosphate (molecule solely responsible for this regulation)
- activates PFK-1 to extent that glycolysis stops without it
Fructose 2,6-phosphate produced and broken down by single bifunctional enzyme with two components:
- phosphofructokinase-2 (PFK-2) = creates fructose 2,6-bisphosphate
- fructose 2,6-bisphosphatase = breaks down fructose 2,6-biphosphate
Glucagon activates fructose 2,6-bisphosphatase and inhibits PFK-2, reducing fructose 2,6-phosphate and downregulating PFK-1 glycolysis
- Makes sense because glucagon levels high when blood sugar levels are low, don’t want to use up that glucose
- want to liberate it into bloodstream for other cells to use
Insulin inhibits fructose 2,6-bisphosphatase and activates PFK-2, increasing fructose 2,6-bisphosphate which activates PFK-1 and stimulates glycolysis (committed step)
- insulin levels are high when blood sugar levels are high, want to be able to break down glucose and harness its energy

Kinases (enzymes)
Add phosphate groups to their substrates
Phosphatases (enzyme)
Remove phosphate groups from substrates
3rd regulatory step in glycolysis
Regulated by?
Final 10th step, phosphoenolpyruvate (PEP) is converted into pyruvate by enzyme pyruvate kinase
- Pyruvate kinase is allosterically inhibited by ATP
- if theres a lot of ATP in the cell, final reaction is inhibited
Pyruvate kinase is also inhibited by acetyl-CoA
- which is derived from pyruvate and long-chain fatty acids, also metabolized for energy
Allosteric inhibition
Allosteric regulation is the regulation of an enzyme by binding an effector molecule at a site other than the enzyme’s active site
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What mechanisms regenerate NAD+ needed for step 6 of glycolsis?
Aerobic respiration: electron transport chain
Anaerobic respiration: fermentation
Parallel pathways
Lactic Acid Fermentation
Occurs in anaerobic cells that never use oxygen and aerobic cells that don’t have access to oxygen for period of time
ex. muscle cells carry out lactic acid fermentation in high intensity exercise; not getting enough O2 and relying on glycolysis
mechanism: single redox reaction where lactate dehydrogenase converts pyruvate to lactic acid
- simultaneously, NADH is oxidized to NAD+ to go back into glycolysis
Fermentation itself doesn’t make any ATP

Ethanol fermentation
Much less common among eukaryotes but famously carried out by yeasts (single celled eukaryotes) – converts sugars into ethanol
- how alcoholic beverages like beer, kimchi, yogurt are made
- Starts with glucose or disaccharide like sucrose (glucose attached to fructose)
- Gets converted to pyruvate through glycolysis (same process so far)
- Then enzyme pyruvate decarboxylase converts pyruvate into acetaldehyde, carbon lost as molecule of CO2
- Alcohol dehydrogenase turns acetaldehyde into ethanol while NADH is oxidized into NAD+ (feeds back into glycolysis)
How can you obtain glucose?
Body can obtain glucose by eating, by breaking down stored glucose - glycogen, or by gluconeogensis

What does gluconeogenesis do and how does it begin?
Gluconeogenesis creates glucose from other biochemical substrates, occurs mainly in the liver (and to a lesser extent in the kidneys)
- Begins with pyruvate from
- protein (glucogenic amino acids = not leucine or lysine)
- glycerol = product from fatty acid breakdown
- lactate from lactic acid fermentation
Gluconeogenesis 1st bypass step (also first step)
Looks like glycolysis in reverse but glycolysis has 3 irreversible steps:
- Pyruvate to PEP takes two steps instead of one in the reversible reaction (10th step of glycolysis); occurs in mitochondria (***to avoid pyruvate from glycolysis being converted back into PEP)
- Enzyme pyruvate carboxylase converts pyruvate into oxaloacetate
- Oxaloacetate briefly converted to malate to be transported out of mitochondria into cytosol then converted back into oxaloacetate
- PEP carboxykinase converts it into PEP
- Enzyme pyruvate carboxylase converts pyruvate into oxaloacetate
Then, follows reverse of glycolysis until has to use enzymes to bypass steps of glycolysis that require ATP input

Gluconeogenesis second, third, and fourth bypass steps (last three steps)
- Fructose 1,6-bisphosphate (product of committed step of glycolysis that requires ATP) is converted to fructose 6-phosphate by enzyme fructose 1,6-bisphophatase (hydrolyzes a phosphate group)
- Fructose 6-phosphate converted into G6P by phosphohexose isomerase (same enzyme from glycolysis)
- Glucose 6-phosphate converted back into glucose by glucose 6-phosphatase (hydrolyzes another phosphate group)
*** only two different steps from glycolysis
Once liver has newly formed glucose, send it out into bloodstream increasing blood glucose conc and for other cells to utilize

Cells capable of performing both glycolysis and gluconeogenesis
Liver and kidney cells, regulate processes so one predominates at a given time
Gluconeogenesis and insulin/glucagon
Like glycolysis, regulated by insulin and glucagon (regulate blood glucose levels in general)
- Insulin- promotes glycolysis, inhibits gluconeogenesis
- secreted when blood glucose is high
- promotes synthesis of fructose 2,6-bisphosphate
- Glucagon- inhibits glycolysis, promotes gluconeogenesis
- secreted when blood glucose is low
- reduces amount of fructose 2,6-bisphosphate incell (inhibitor of fructose 1,6-bisphosphatase/gluconeogenesis)
Regulation of gluconeogenesis
Occurs at steps where gluconeogenesis bypasses the irreversible steps of glycolysis; only need to focus on two
- First step - 2 step pyruvate to PEP through oxaloacetate
- cell has choice - push pyruvate through gluconeogenesis to make glucose or through mitochondria/aerobic respiration to make ATP
- to make energy, converts pyruvate into acetyl CoA in mito
-
acetyl CoA regulates gluconeogenesis this way; if there’s plenty, downregulates conversion of pyruvate into acetyl CoA
- causes pyruvate to build up in cell and go to gluconeogenesis
- cell has choice - push pyruvate through gluconeogenesis to make glucose or through mitochondria/aerobic respiration to make ATP
- 9th step (fructose 1,6-bisphosphate to fructose 6-phosphate by enzyme fructose 1,6-bisphosphatase)
- committed and rate limiting step of glycolysis
- step where balance between gluconeogenesis and glycolysis is maintained
- Fructose 1,6-bisphosphatase enzyme is inhibited by AMP
- high levels of AMP signal the cell is low on energy –> glycolysis
- Fructose 1,6-bisphosphatase enzyme is inhibited by AMP
- In addition, regulatory compound fructose 2,6-bisphosphate also inhibits fructose 1,6 bisphosphatase enzyme
- *** high levels of fructose 2,6-bisphosphate activate glycolysis and inhibit gluconeogenesis
- 9th step (fructose 1,6-bisphosphate to fructose 6-phosphate by enzyme fructose 1,6-bisphosphatase)
Mitochondria structure
Double membrane - two separate lipid bilayers with space between them
Inner and outer mitochondrial membrane
Intermembrane space in between them
Mitochondrial matrix is innermost region in inner mito membrane
Outer mitochondrial membrane
Highly porous, studded with membrane proteins called porins which allow hydrophillic molecules and even ions to move freely in and out by diffusion
Inner mitochondrial membrane
impermeable to almost everything but water and small gas molecules (oxygen and carbon dioxide)
- larger molecules can only enter through special transport proteins
- has incredible surface area; 5x as large as outer membrane
- has to be folded, folds are called cristae
Also contains embedded proteins of the Electron Transport Chain (produce most of cell’s ATP)

Intermembrane space (mitochondria)
Compartment tends to be acidic due to protons being pumped from innermost region into intermembrane space
Mitochondrial matrix
Innermost region, contains:
- citric acid cycle enzymes
- electron carriers
- mitochondrial RNA and DNA
- ribosomes
Metabolism in aerobic cells
- Glucose broken down into pyruvate by glycolysis
- Pyruvate enters mito matrix by pyruvate dehydrogenase complex
- Pyruvate converted into acetyl CoA in mitochondria
- Acetyl CoA enters the Citric Acid Cycle (Krebs/TCA (tricarboxylic acid))
- Citric Acid Cycle not just next step after glycolysis, but crossroads for other metabolic pathways; non-carbohydrate precursors can get fed into it at certain steps and its intermediates can go take part in other anabolic process - Citric Acid Cycle produces reduced electron carriers NADH and FADH2 which are used to produce energy in oxidative phosphorylation
Pyruvate Dehydrogenase Complex
Embedded in inner mitochondrial membrane
- Converts pyruvate –> acetyl CoA by decarboxylation (oxidation) as pyruvate crosses inner mito membrane
- also produces one NADH (corresponding reduction)
3 different enzymes physically linked together so their reactions happen efficiently and in sequence
- Pyruvate dehydrogenase
- Dihydrolipoyl transacetylase
- Dihydrolipoyl dehydrogenase
Also requires help from 5 coenzymes: thiamine pyrophosphate, FAD, NAD, Coenzyme A, and lipoate
Produces two NADH per glucose

decarboxylation
Removal of a carboxylic acid group
What is acetyl CoA
Two carbon compound linked through a sulfur atom to larger molecule coenzyme A-
Involved in pyruvate dehydrogenase complex,
- Derived from fatty acid oxidation and the breakdown of certain amino acids
Main entry point of Citric Acid Cycle

Citric Acid Cycle basics
Citric Acid Cycle not just next step after glycolysis, but crossroads for other metabolic pathways; non-carbohydrate precursors can get fed into it at certain steps and its intermediates can go take part in other anabolic process
Generates some ATP directly through production of GTP, main goal is to produce reduced electron carriers NADH and FADH2 – used later to produce energy through oxidative phosphorylation
Called a cycle because it regenerates the compound it starts with, can continue steps as long as acetyl CoA is inputed
Where does Citric Acid Cycle occur?
- in aerobic prokaryotes with no mitochondria, Citric Acid Cycle occurs in cytoplasm; in eukaryotes, takes place in mitochondrial matrix
Citric Acid Cycle steps
- Acetyl CoA joins with 4-carbon oxaloacetate to form 6-carbon citrate
- citrate undergoes redox and decarboxylation reactions to form products of CAC
- Final product is oxaloacetate, joins with acetyl CoA to start process again
- Acetyl CoA joins with oxaloacetate to form citrate (deprotonated form of citric acid)
- reaction catalyzed by citrate synthase; energetically favorable/irreversible
- Citrate converted to cis-Aconitate and then Isocitrate by enzyme aconitase
- reversible, moves hydroxyl group
- Isocitrate converted to oxalosuccinate and then a-ketoglutarate
- enzyme isocitrate dehydrogenase
- **releases CO2 (first carbon lost)(one reason we exhale carbon dioxide as waste)
- One molecule of NADH produced; rate-limiting and irreversible
- a-ketoglutarate converted into succinyl CoA by a-ketoglutarate dehydrogenase
- **also produces one NADH and loses one CO2
- have lost both acetyl CoA carbons
- Succinyl CoA converted to succinate by
- succinyl-CoA synthetase
- produces molecule of GTP through substrate level phosphorylation
- Succinate converted into fumarate
- by enzyme succinate dehydrogenase
- produces FADH2
- Fumarate oxidized by fumarase into malate
- Malate is recycled back into oxaloacetate by malate dehydrogenase
- produces one more NADH
- thermodynamically unfavorable but progresses due to Le Chateliers principle because oxaloacetate is used up quickly
Citric Acid Cycle products
Products are per pyruvate, double them to get products per glucose:
Per pyruvate:
From pyruvate dehydrogenase complex: 1 NADH
From citric acid cycle:
1 GTP (can be used directly as energy)
3 NADH
1 FADH2
2 CO2 (waste product)
Electron transport chain (what it consists of, what it does, what it produces)
Consists of 4 membrane bound protein complexes (I, II, III, IV) located on innermembrane in eukaryotes
Harvest electrons from electron carriers NADH and FADH2 in a set of reactions that also pumps H+ into mitochondrial intermembrane
- uses electrons to drive production of energy in form of ATP via oxidative phosphorylation
- electrons ultimately converted to water via redox reaction

Oxidative phosphorylation (what it’s used for, steps)
Used in mitochondria for forming ATP
- Electron transport chain pumps H+ into inter membrane space of mitochondria
- H+ diffuse down concentration gradient into matrix powering ATP synthase (embedded in inner membrane, synthesizes ATP)
- Electrochemical energy stored in charge differential between inter membrane space and matrix produces ATP
Per glucose molecule… (products through all metabolic processes)
2 ATP from glycolysis; 2 NADH
0 ATP from PDC, 2 NADH
2 GTP from citric acid cycle; 6 NADH; 2 FADH2
(10 NADH x 2.5 ATP) + (2 FADH2 x 1.5ATP) = 28 ATP from oxidative phosphorylation
32 ATP total per glucose but had to use 2 ATP to get pyruvate from cytoplasm so really 30 ATP
In aerobic prokaryotes, electron transport chain protein complexes are located…
In cell membrane
Electron transport chain complex reduction potentials
Each electron carrier (I, II, III, IV) has more positive reduction potential than the one before it - series of redox reactions
- more positive reduction potential means compound wants to be reduced more (wants electrons more, keeps them moving consistently)
- as electrons pass from carrier to carrier, energy is used to pump protons across inner membrane into matrix producing proton gradient used to power oxidative phosphorylation
- ends with oxygen, final electron acceptor, has highest reduction potential in ETC
- picks up two protons and is turned into molecule of water x2
- ** why aerobic respiration requires oxygen
Summarize ETC as set of redox reactions that transfer electrons from NADH and FADH2 to O2, reducing it to water
H’s from NADH and FADH2 are broken off as H+ protons and electrons
Two different pathways electrons can take through ETC: NADH pathway
- NADH from glycolysis, PDC, and CAC drops off two electrons at complex I (NADH dehydrogenase) -> NAD+
- Electrons transferred to electron carrier ubiquinone, reducing it to ubiquinol
- ubiquinone = ketone, ubiquinol = alcohol
- Energy from this reaction harnessed by complex I to send 4 protons (H+) across the matrix into intermembrane space
- Ubiquinol bypasses complex II and transfers electrons to carrier cytochrome C, which can only carrier one electron - so theres two cytochrome C’s
- (hemeprotein, core component is Fe, alternates between Fe+2 and Fe+3)
- During which, complex III sends four more H+’s into intermembrane space
- Ends at complex IV which pumps two H+’s, where cytochrome C’s transfer electrons to oxygen reducing it to water
FADH2 electron transport chain pathway
Each acetyl CoA through CAC gives rise to one FADH2 which remains connected to enzyme that produced it, succinate dehydrogenase which is also complex II of ETC
- important point of overlap between CAC and ETC
- electrons from FADH2 enter at complex II instead of complex I
Complex II doesn’t pump any protons into intermembrane space, means less ATP can be generated than from NADH (1 NADH ~ 2.5 ATP, 1 FADH2 ~ 1.5 ATP)
Otherwise, path is the same as electrons after they go through complex I from NADH
Proton motive force
Proton gradient created from protons being pumped out of matrix into intermembrane space
Entrapped protons want to move back into matrix to dissipate their charge and concentration gradient = stored electrochemical energy
- However, inner membrane is impermeable to ions, have to reenter through ATP synthase
- uses flow of protons to power formation of ATP from ADP and inorganic phosphate (Pi)
Why would we need regulation of aerobic respiration (CAC and ETC)
Already have plenty of ATP available or not enough oxygen available; lots of ADP upregulates
Where does regulation of aerobic respiration occur
CAC and ETC work simultaneously
If plenty of energy, best way to downregulate is at the entry point to prevent both processes from happening = at pyruvate dehydrogenase complex (PDC)
Regulation can also occur in 3 steps of Citric Acid Cycle

Upregulation of aerobic respiration
When there are high levels of coenzyme A, AMP, and NAD+, indicates cell needs more energy and PDC is upregulated to produce more acteyl CoA
Downregulation of aerobic respiration
- When cell has high levels of ATP, NADH, and acetyl CoA it downregulates PDC
- feedback inhibition
- High levels of fatty acids can also downregulate PDC
- fatty acids metabolized into acetyl CoA
- High levels of fatty acids can also downregulate PDC
Regulation in Citric Acid Cyle (respiration regulation)
3 key steps regulated:
- First step when acetyl-CoA and oxaloacetate combine to form citrate upregulated by ADP, downregulated by ATP and NADH
- also inhibited by citrate and succinyl-CoA, intermediates downstream of reaction
- Conversion of isocitrate to alpha-ketoglutarate is downregulated by ATP, upregulated by ADP
- Formation of succinyl-CoA is inhibited when cell has too much succinyl-CoA or too much NADH
**Pattern - energy production steps upregulated by compounds that suggest cell needs more energy, downregulated by cells that indicate cell has enough
Disruption of Cellular Respiration processes
Several drugs and toxins interfere with electron transport chain
ex. cyanide inhibits cytochrome C oxidase, enzyme that transfers electrons to oxygen, shuts ETC down
Can be fatal
Quantitative experimental methods
Generate numerical data
- always produce numbers as results
- categorized, ranked, or used to construct graphs and draw statistical conclusions
Qualitative experimental methods
Not numbers; words, opinions, observations, anything not numerical
- more open-ended, exploratative
- cannot be easily quantified
Usually when there’s not much prior research on a topic
Mixed research methods
Mix of both qualitative and quantitative methods
- ask participants to eat a certain number of donuts, then describe their feelings
Objective experimental measures
Unbiased
Fact-based
ex. height
Subjective experimental measures
Subject to opinion
No right or wrong answer
ex. how comfortable do you feel right now
Validity
The extent to which a studys results are both genuine and generalizable
- How do we know results are accurate?
- How do we know that our results will apply to the “real world” rather than being specific to that experiment?
Accurate results
Internal validity
Draw causal conclusions - minimize confounding variables
manipulating X caused a change in Y
confounding variable- outside factor not being study that impacts both variables
- can lead to incorrect conclusions
External validity
Extent we can generalize results (to different experimental realizations or real life)
Test validity (4 types)
Tests what it intended to
- construct validity- assesses construct designed to test
- content validity- how well test covers full scope of content intended to measure
- criterion validity- how well test correlates with well-respected criterion
- predictive validity- focuses on future events
Reliability
Extent to which study results are consistent when repeated
- if we do same study over again, is there a positive correlation between them
Precision
The extent to which experimental measurements agree
- Refers to data points
Accuracy
The extent to which measurements agree with standard/correct values
- Data points
- Validity
4 experimental study scenarios
-
Reliable and valid- experiment yields consistent values close to the true value
- ideal scenario
-
Unreliable and invalid- repeating the experiment yields inconsistent values
- results not close to true value
- Reliable and invalid- data points clustered closely around an inaccurate value
- Unreliable and valid- results all over the place but average is close to true value
Reliability and validity
Characteristics of a study
Precision and accuracy
Characteristics of a data set
Survey methods
- Collect large amounts of data
- Often take form of questionnaires
- Participants must be representative of population intended to study
- Normally inexpensive and easy to implement; can reach large sample
- **Problems can arise from bias
Questionnaires
Form of self report - participant responds without interference
- Often use Likert scales- statement followed by continuum of possible responses (ex. from 1-5, strong disagreement to strong agreement)
Self-reporting bias (survey methods)
aka Response bias
(two types)
Bias inherent to survey method; natural side effect of allowing participants to choose their responses
- social desirability bias- answer in a way that makes oneself appear more successful
-
acquiesence bias- tendency to answer yes when asked a question, especially when uncertain
- can counter by including survey items with opposing meanings
Mutations and how they can arise
Mistakes in DNA coding; can affect corresponding mRNA and by extention amino acid sequence and protein final product
- can arise when a cell is exposed to a DNA-damaging agent, or mutagen
- some can be deleterious and some can be beneficial, driving evolution
Mutagens
DNA-damaging agent; not always harmful
-
physical mutagens- heat and radiation
- ionizing radition
- UV light
-
chemical mutagens- base analogs
- reactive oxygen species (ROS)
- biological agents- viruses, bacteria, transposons
(add more to this)
Common examples of reactive oxygen species
Peroxide, superoxide, hydroxyl radical
Contain lone electrons which make them especially reactive (would much rather exist in pairs)
Spontaneous mutations
Occur in cells not exposed to mutagenic agents
ex. mistakes in DNA replication
Base pair substitution mutation and 3 potential effects
Bases substituted for one another
- can impact at most one codon and therefore one amino acid
3 potential effects:
- silent mutation- no effect on amino acid sequence
- missense mutation- replaces an amino acid
- nonsense mutations- creates a stop codon
Insertion/deletion mutation
Bases inserted into sequence (one or more) or bases deleted from sequence (one or more)
- can cause frameshift mutation: can change every subsequent codon in a sequence
- if number of bases inserted or deleted is a multiple of three, reading frame won’t shift
Silent mutations
Don’t change organisms phenotype
- genetic code degeneracy: multiple codons can code for same amino acid
Missense mutations (2 types)
Amino acid is changed when DNA sequence is translated
-
conservative- new amino acid has similar structure to old, partially conserve original function
- ex. threonine to serine
- minimal effects
-
nonconservative- replaces original amino acid with one with very different structure
- threonine to proline
- can greatly impact final protein

Nonsense mutations
Codon for an amino acid replaced with a stop codon; either UGA, UAA, or UAG
- truncates (shortens) protein, typically rendering it nonfunctional
Pyrimidine dimer mutation
UV light; cytosine or thymine bases on SAME strand bind together
Point mutations
Change to a single nucleotide
Can be subsitution, insertion or deletion
Loss of function mutations
Partially or entirely prevent a protein from functioning correctly
Gain of function mutation
Protein takes on new function that it didn’t have prior to mutation
Chromosomal abnormalities (6)
Deletion, duplication, inversion, insertion, translocation, aneuploidy
- Deletion, duplication, and inversion take place on single chromosome
- Translocation and insertion tend to impact two chromosomes
Chromosomal deletion
Removal of a segment of genes on a chromosome
- makes chromosome shorter
- what happens when a gene is deleted depends on allele on other chromosome
- depends on genotype
- ex. two alleles for brown hair color, if one gets deleted, may result in no change but transcribe less mRNA and make less protein corresponding to this hair pigment
- if alleles are different, could change hair color
- depends on genotype
Chromosomal duplication
Segment of a chromosome is copied; two copies of one allele on same chromosome
- generally results in more mRNA and protein corresponding to genes on duplicated segment
Chromosomal inversion
Reversal in directionality of segment of DNA on chromosome
- unlike duplication and deletion, doesn’t change gene dosage
- many have no noticeable effects
Chromosomal insertion
Chromosomal translocation
Genetic material from one chromosome is exchanged with genetic material from another
-
balanced transloaction- doesn’t result in lost or extra genes
- typically harmless
- may produce gametes with imbalances in the genetic material present which can cause child to have unbalanced translocation
- unbalanced translocation- results in lost or extra genes

Chromosomal insertion
One way transfer- part of a chromosome breaks off and inserts itself in sequence of second chromosome
Chromosomal transposition
Transposons- noncoding genetic elements that can initiate their own movement from chromosome to chromosome
- over 40% of human genome
- generally not problematic unless they insert in coding sequence of a gene
- don’t translocate since movement is one way
Chromosomal aneuploidy
Abnormal number of copies of a chromosome within a cell
- typical human cells have 23 pairs of chromosomes
- 22 autosomes and one sex chromosome pair
trisomy- extra copy of a chromosome
- trisomy 21- down syndrome
monosomy- one copy of a chromosome
**Typically results from nondisjunction, failure of chromosomes to segregate during anaphase of meiosis or mitosis
- risk increases with maternal age (older eggs)
DNA repair
1 error per 1 billion bases - 6 billion base pairs per cell = ~6 errors per DNA replication
DNA polymerase proof reading- mistakenly added base becomes paired with a non-complimentary base on opposing strand
- hydrogen bonding between mismatched bases is unstable; detected by DNA pol
- removes base pair and reinserts correct base
also known as 3’-5’ exonuclease activity
Mismatch repair
If DNA polymerase misses an error while proofreading
Immediately after DNA replication and through G2 stage, excision of base occurs
- base is party of newly replicated strand, so mismatch repair can distinguish new from old by DNA methylation
Functions only during replication
Base excision repair
Removes a single erroneous base, limited to small scale errors
** non replicative errors
Nucleotide excision repair
Removes multiple bases, can fix larger mutations
- ex. pyrimidine dimers
Biological signals
Chemical- how cells respond to surrounding, communicate with other cells, and alter their own internal environments
Electrical
Mechanical
Biochemical signals
How cells respond to surrounding, communicate with other cells, and alter their own internal environments
-
hormones
- peptide, steroid, or amino acid-derived molecules
- travel through circulatory system to exert effects on target cells
- peptide, steroid, or amino acid-derived molecules
-
cytokines
- small proteins that modulate immune responses
-
neurotransmitters
- chemicals that transmit information between neurons
Biochemical classes
- Lipids
- Amino acids
- Proteins
- Gases
- neurotransmitter nitric oxide
Types of Signaling
-crine
Differentiate terms by how far they travel through the body
-
intracrine signals travel the shortest distance
- signals act within the cell that synthesizes them
- autocrine signals are released, then bind to receptors on the cell that synthesized them
-
juxtacrine
- signals travel between cells in close contact
-
paracrine
- signals travel between nearby cells
endocrine- signals (hormones) travel between distant cells via circulatory system

Sugar consumption promotes release of
Insulin, a hormone that is an endocrine signal
Inflammation involves the release of
Cytokines; affect nearby cells via paracrine signaling
- cells respond to fight infection or promote wound healing
Cocaine use affects…
Release and reuptake of multiple neurotransmitters (also technically paracrine signalling molecules; secreted by one neuron and act on a neighboring neuron)
When signaling molecule binds to a receptor, it is a…
When it binds to the receptor, it triggers…
Ligand
An action that affects the target cell
First messengers
Second messengers
Ligand (signal molecule) that binds to receptor on cell surface, initiates signaling pathway
Receptor triggers release of another biosignal in the cell
- common secondary messengers are calcium ions and cyclic adenosine monophosphate (cAMP)
Types of receptors
Membrane receptors- attached to plasma membrane; often contain one at least one transmembrane domain
- protein domain which passes through the cell membrane; mostly made of hydrophobic amino acids
- can only relay messages originating outside of the cell to the interior of the cell
- bind polar proteins
- charged or have a lot of polar functional groups
Nuclear receptors- found in cytoplasm or nucleus
- bind to nonpolar, lipid-based ligands
- steroid or thyroid hormones
- can diffuse directly through membrane
- Once ligand binds, ligand-bound receptor migrates to the nucleus if its not already there
- function as transcription factors, regulate rate of transcription
Types of membrane receptors (3)
-
Ion channel linked (aka ligand gated)
- Enzyme channel linked
-
- G-protein coupled receptors
Ion channel-linked (aka ligand gated)
- contain transmembrane pores that allow ions to pass through when channel is open
- for channel to open, receptor must be bound by ligand
- found on neurons, ligand is usually a neurotransmitter such as acetylcholine
- if cell becomes more positive as a result, moves closer to electrical threshold, more likely to fire action potential
- “depolarizes” neurons (aka excited)
- efflux of negative ions from cytoplasm also depolarizes neurons
- If movement of ions makes neuron more negative (like chloride ions), its moved further away from firing potential
- inhibited, hyperpolarized
Enzyme linked (catalytic) receptors
Either enzymes themselves or directly associated with enzymes they activate
- most commonly these enzymes are protein kinases, which phosphorylate (add a high energy phosphate group)
-
Receptor Tyrosine Kinase (RTKs)
- surface receptors for a bunch of hormones and growth factors
- play a key role in cell growth when functioning properly
- when not functioning properly, can contribute to a number of diseases (cancer)
G-coupled receptor (GPCR)
- protein located in the cell membrane that binds extracellular substances and transmits signals from these substances to an intracellular molecule called a G protein (guanine nucleotide-binding protein).
Gases
Play key roles in many biological processes: O2, CO2, Nitric oxide (cell signaling molecule)
Expandable and compressible, can change volume (unlike solids and liquids
Kinetic Molecular Theory, Ideal Gases
Kinetic Molecular Theory
Gas can be understood as a system of tiny particles bouncing around inside a given region of space
- pressure on the walls of container is a result of elastic collisions of the particles with those walls
- Average kinetic energy is proportional to the temperature of the gas
-
U = 3/2kT
- U = avg kinetic energy (1/2mv2)
- k = a constant
-
U = 3/2kT
Brownian motion= couldn’t see gas particles but could see random jittery movement of pollen grains under light microscope, caused by movement of gas molecules
Ideal Gases
Simplified manageable model of how gases behave:
- **Core assumptions:
- Gas particles have no volume
- Gas particles experience no attractive or repulsive forces
**Higher temp, high volume, and low pressure makes gases behave more ideally
- Minor assumptions:
- collisions are perfectly elastic
- motion is random
Temperature conversions
Boyle’s Law
Pressure and volume of a gas are inversely related
- P1V1 = P2V2
- or PV = constant (classic inverse relationship)

Charles’ Law
Volume and temperature of a gas are directly related
Increased temperature expands its volume
ex. take air out of your tires in heat
- V1/T1 = V2/T2
- V1/T1 = k (constant) (classic direct relationship)

Avogadro’s Law
Volume of a gas is directly related to the number of moles of gas particles
- V1/n1 = V2/n2
Any two containers of gas with same volume will have same number of moles with same temperature and pressure, despite atom size (ideal gas law)
**Molar volume: 1 mole = 22.4 L at 273 Kelvin and 1 atm
(STP = standard temperature and pressure)
Ideal gas law
PV = nRT
- R = ideal gas constant = .08206 L atm/mol K (use .08)
- or
- 8.314 J/ mol K
- ** values will be given on MCAT
Real Gases equation
Gas particles do have a size and may be intermolecular forces between them
- Van der Waals euqation: modified ideal gas law
- (P + a/V2m)(Vm - b) = RT
- Volume - b is taking account for gas particle size
- Pressure is modified by “a”, a constant for each gas and Vm its molar volume
** Really polar molecule has larger “a” term, behaves more non-ideally; larger gas particles behave less ideally
At large volume, is ideal gas pressure or real gas pressure higher?
At smaller volumes with higher molar concentrations of gas, is ideal pressure or real gas pressure higher? (under extreme conditions)
Ideal gas because real particle size still negligible but attractive forces bring particles together
Real gas pressure is higher
Daltons Law of partial pressures
Ptotal = P1 + P2 + P3…
Pressure that a gas exerts is independent of other gases present, depends on total pressure and mole fraction of gas
Mole fraction (Xn) = ngas/ntotal = Pgas/Ptotal
***Pgas = (Xgas)(Ptotal) - to get partial pressures
Mole fraction
(Xn) = ngas/ntotal
Graham’s law of effusion
When a gas is effusing (escaping from a small opening), smaller lighter particles escape faster
Rate 1/ Rate 2 = √((molar mass 2)/(molar mass 1))
Respiratory sytem flow/anatomy
- Air enters oral cavity (nostrils/nares)
- nasal cavity behind nostrils has a mucus membrane with tiny hairs called vibrissae that help filter particulate matter for first line immune defense (sneezing)
- Air passes the pharynx at the back of the mouth and path diverges into the trachea and esophagus
- epiglottis is a flap of cartilaginous tissue, covers and protects trachea when swallowing, shunting food toward esophagus
- opens to allow air to flow into trachea during breathing
- Air then passes the larynx, which contains the vocal cords
- vocal cords vibrate when air moves over them, consciously controlled during speaking/singing
- Air continues down trachea, lined with ciliated epithelial cells and mucous producing goblet cells
- mucous traps stray bacteria/particulate matter, thrust upward by cilia to be expelled/swalled as phlegm
- Trachea splits into two main bronchi, which themselves split off into bronchiole
- if bronchi become infected = bronchitis
- if bronchioles become infected = bronchiolitis
- Smallest bronchioles terminate in air sacs known as alveoli
- where gas exchange occurs between alveoli and their capillaries
- 500 million alveoli for surface area
- alveoli very delicate, covered with surfactant, breaks up and reduces surface tension

Epithelial cells
Endothelial cells
Goblet cells
Alveoli
- Smallest bronchioles terminate in air sacs known as alveoli
- where gas exchange occurs between alveoli and their capillaries
- 500 million alveoli for surface area
- alveoli very delicate, covered with surfactant, breaks up and reduces surface tension
If alveoli become infected = pneumonia
Lungs are one of last forming organs in developing fetus, so premature birth gives risk to neonatal respiratory distress system – lungs collapsing due to insufficient surfactant production
- readily treatable by administering surfactant artificially until lungs are developed

Gas Exchange in Respiration
Specialized alveoli
- alveolar wall is one cell thick, oxygen from air entering lungs diffuses readily across the membrane into alveolar capillaries
- blood in alveolar capillaries just returned from systemic circulation (CO2 rich, oxygen poor)
- oxygen diffuses from alveoli down concentration gradient, CO2 follows concentration gradient into the alveoli
- epelled from body during exhalation
- oxygen diffuses from alveoli down concentration gradient, CO2 follows concentration gradient into the alveoli
- Oxygen entering blood quickly latches onto hemoglobin, oxygen carrier

Lungs
Delicate, which is why they’re enclosed by a ribcage
- within thoracic cavity, lungs encased in two serous membranes
- parietal pleura- lines the thoracic wall
- pulmonary pleura- adheres to the lung
- space between them is the pleural cavity
- during inhalation, muscular diaphragm beneath the lungs contracts, thoracic cavity expands –> reduced pressure in the pleural cavity causing lungs to expand
- pressure and volume relationship
Negative pressure breathing
Gases equalize pressures between regions of space; since volume and pressure have inverse relationship, increased lung volume reduces alveolar pressure
- causes air to flood the lungs to maintain equilibrium with ambient air
- lung air pressure becomes “negative” relative to ambient, forcing air to follow its pressure gradient
P1V1=P2V2
Breathing
Can be voluntary or involuntary
- involuntary controlled by medulla oblongata of the brain system
Inhalation always an active process; downward contraction of the diaphragm requires energy
Exhalation is typically passive, but can be active
- abdominal muscles and internal intercostal muscles can produce more forceful
- such as during exercise
Respiratory volumes
Lungs capable of adapting to situations where oxygen needs are increased
Tidal volume- normal breathing
Inspiratory reserve volume- any additional air we could inhale
Expiratory reserve volume- any additional air we could exhale
Total lung capacity- total volume our lungs can hold
Vital capacity- maximum volume of air we could exhale
Residual volume- air remaining in lungs that can’t be exhaled (remains in alveoli so lungs don’t collapse completely)
Use of respiratory volume metrics
Evaluating patients with pulmonary diseases like emphysema, COPD
Respiratory immune defense
- Hair follicles in nose, cilia lined epithelial cells trap particulate and microbes
- expelled by sneezing or cilia pushing mucous upward then coughing or swallowing
Respiratory tract also produces antimicrobial proteins called defensins, fight against bacteria, fungi and viruses
Loss of cilia from extensive exposure to cigarette smoke, increasing risk of infection
Respiratory contribution to thermoregulation
Vessels in nasal cavity and trachea dilate in hot conditions to increase surface area through which heat can be radiated and lost to the environment
Constrict in cold conditions to retain heat as blood passes through
- These capillary beds can be sensitive; injury or dry conditions that cause mucous membranes to crack can cause nose bleeds
- Rely more heavily on other thermoregulation mechanisms, like sweating
- Furrier mammals can’t sweat to same extent, rely on panting/rapid breathing to lose heat via evaporative cooling
Bicarbonate Buffer for circulation
- Carbon dioxide participates in equilibrium with carbonic acid and bicarbonate ions
- Largely travels through the bloodstream in the form of bicarbonate
In equation, elevated CO2 directly translates to increased H+ concentrations, which acidifies the blood –> buffer system that helps maintains blood pH at ~7.4
- pH lower than this would be acidemia, higher pH would be alkalemia

Peripheral chemoreceptor pathway
Chemoreceptors in the peripheral and central nervous systems detect oxygen, CO2, and H+ concentrations in the blood
- why we feel urge to breath when we hold our breath, depleting oxygen and allowing CO2 and H+ to build
- in response, our respiratory rate speeds up to accelerate removal of CO2 and replenish O2 and return blood pH to normal
*
- in response, our respiratory rate speeds up to accelerate removal of CO2 and replenish O2 and return blood pH to normal
Blood circulates:
Oxygen
Nutrients
Essential ions
Proteins
Fluids
Metabolic wastes
If you put blood in a centrifuge, it separates into:
-
Plasma- fluid component of blood
- 55% volume
-
Buffy coat- contains white blood cells and platelets (appears white)
- 1% volume
-
Erythrocytes (red blood cells)- carry gases, specifically oxygen and carbon dioxide
- usually around 45% = hematocrit

Plasma
- fluid component of blood
- about 55% of blood volume; carries ions, proteins, nutrients and gases
- exercise can increase plasma volume to help circulate gases more readily
Buffy coat
- contains white blood cells and platelets (appears white)
- 1% of total volume
- leukocytes: white blood cells, immune cells
-
platelets: cell fragments from specialized cells called megakaryocytes
- no nucleus
- essential to coagulation (blood clotting);
-
platelets: cell fragments from specialized cells called megakaryocytes
Coagulation Cascade
Clotting factors lead to a molecule called prothrombin being converted into thrombin
- thrombin converts fibrinogen into fibrin, a fibrous molecule that forms skeleton of a blood clot
- platelets then pile on top to form a platelet plug
Clot disintegrates as the wound heals – can sometimes not disintegrate and get lodged somewhere else
Thrombosis and Thromboembolism
Blood clot doesn’t disintegrate and gets lodged somewhere else
- if occurs in the heart, can lead to heart attack
- in the brain, can result in a stroke
Hemophilia
Missing one of the factors required to form blood clots, more susceptible to excessive bleeding
Erythrocytes
Red blood cells, carry CO2 and oxygen in the blood by carrying millions of copies of hemoglobin molecules
Produced in red bone marrow of flat and long bones, just like white blood cells
- body releases a horomone called erythropoietin (EPO) from the kidneys to stimulate production
- (can inject in yourself for blood doping)
- 45% of volume of blood
- hematocrit- proportion of your blood that is composed by red blood cells
Just as they are about to mature to adult red blood cells, erythrocyte cells eject their nucleus and other organelles
- makes them extremely energy efficient, but can’t live very long (~120 days)
- sent to the spleen for destruction
Spleen function
it fights invading germs in the blood (the spleen contains infection-fighting white blood cells) it controls the level of blood cells (white blood cells, red blood cells and platelets) it filters the blood and removes any old or damaged red blood cells.
Erythrocytes (red blood cells) coat themselves with
Glycoproteins (sugar-coated proteins) on cell surface
ABO blood typing is based off which ABO glycoproteins are expressed on a person’s red blood cells
- depends on persons genotype
- A antigen = blood type A
- B antigen = blood type B
- both = AB
- neither = blood type O
Blood type alleles
AB = codominance, both alleles expressed

Blood type is important because
Immune system produces antibodies against ABO blood types we don’t produce
- A blood type produces anti-B antibodies
- O blood type produces anti-A and anti-B antibodies
O blood type
Universal donor; doesn’t contain any ABO antigens
People with O type can only receive O type
Rh factor
Antigen that can be expressed on red blood cells
- either Rh+ or Rh-
A+ means you have A antigen and Rh factor antigen
If an expecting mother is Rh- and her fetus is Rh+, her immune system makes anti-Rh antibodies that may attack her fetus
- mother is given anti-Rh antibodies preventing her immune system from needing to make its own
Two parts of circulatory system
Heart pumps ~2000 gallons of blood a day
- Systemic- takes oxygen rich blood to bodys tissues then returns oxygen depleted blood back to heart
- Pulmonary- circulatory system through the lungs
Pulmonary circulation
Blood flows through vessels adjacent to alveoli (air sacs) of the lungs; oyxgen from the lungs flows across into the blood vessels while CO2 flows into the lungs to be exhaled
- oxygenated blood returns to the heart, which is pumped back into systemic circulation
3 types of blood vessels
Arteries, capillaries, veins
Arteries
Carry blood away from the heart
- Not always oxygenated, pulmonary artery carries deoxygenated blood from heart to lungs
- Umbilical arteries carry deoxygenated blood from fetus to placenta; becomes oxygenated and back to fetus
Thick muscular walls
Adaptable; vasoconstriction to certain parts of body and vasodilation to others when needed(like fight or flight)
Aorta: body’s largest artery, from left ventricle to rest of body
Arterioles
Arteries branch off into smaller arteries called arterioles; this is where blood pressure begins to lower
Arterioles lead to capillaries
Capillaries
Branch off from arterioles; very small and thin - walls are one cell thick of endothelial cells
- red blood cells file through them one by one
- creates ideal environment for gas exchange to occur across thin capillary walls
- oxygen flows into tissues and CO2/urea into the blood
Very small but so many of them that cross sectional area is greater than any other point in circulatory system = slowest blood velocity
Delicate; blood spilling out causes bruising
Veins
Carry blood towards the heart
- branch off as venules from capillary beds and merge into veins which connect directly to the heart
Thinner, less muscular walls than arteries do; blood pressure is lower than arteries
- working against gravity – require one way valves towards heart preventing backflow
- also rely on skeletal muscles to squeeze veins

Arteries and veins have 3 layers:
- Tunica externa- outermost layer
- Tunica media- middle layer of smooth muscle
- Tunica intima- innermost layer, endothelial cells
1 cause of death in the United States
Cardiovascular disease
Pathogenesis
Manner of development of a disease
Atherosclerosis
Fatty plaques can build up in arteries, making it more diffficult for blood to reach body tissues
In the heart, can lead to heart attack
Heart’s chambers
Right and left atria- two chambers on the top
Right and left ventricles- two chambers on the bottom

Atria chambers
Collecting chambers; blood enters from systemic and pulmonary systems
- Funnel blood into the ventricles
- Right atrium- deoxygenated blood from systemic circulation
-
Left atrium- receives oxygenated blood from pulmonary veins
- funnels blood into left ventricle
Ventricle chambers
Blood funneled in from atria; thick, muscular walls that contract to eject blood out of the heart
Right ventricle- pumps deoxygenated blood through pulmonary artery into the lungs
- blood gets oxygenated, pumped through pulmonary veins back into left atrium of heart
Left ventricle- pumps blood through the aorta, body’s largest artery, to the rest of the body
Inferior and superior vena cavae
Return deoxygenated blood to the right atrium
Atrioventricular valves
Control blood flow between atria and ventricles
- Triscupsid valve (right side)
- Bicuspid valve (mitral)(left side)
Aortic and Pulmonary valves
Between ventricles and their respected arteries
Systole
Diastole
When ventricles contract (blood pressure skyrockets)(peak)
Heart relaxes (blood pressure drops back down)(lower)
blood pressure
Systole / diastole
- healthy is usually under 120/80 mmHg
In a capillary bed, plasma is often…
Forced into spaces between cells and picked up by lymphatic capillary to return to circulation
Heart and nervous system
Sympathetic and parasympathetic effect
Hormones and heart rate
Heart receives signals from nervous system to slow down/speed up but heart can beat on its own due to its own electrical system
- Without nervous system, heart would be oblivious to environmental and chemical cues
- Sympathetic (fight or flight): can speed up heart rate
- Parasympathetic (rest/digest): can slow down the heart rate
Heart rate can also be increased by hormones epinephrine and norepinephrine from adrenal medulla
Heart’s electrical system
Starts wtih Sinoatrial (SA) node- instructs atria to contract and send blood to ventricles
- signal travels from SA node to AV node
Atrioventricular node (AV)- sits at junction between AV and ventricles, helping transmit signal to ventricles
- signal transmitted to Bundle of His and Purkinje fibers
- ventricles contract to push blood out and into sytemic and pulmonary circulation
Gap junctions
Allow flow of?
Located in?
Membrane ion channels, allow ions to flow between individual muscle cells
- all fibers depolarize and contract at the same time
Located in intercalated discs: structures that connect neighboring cardiac muscle cells

Sinoatrial node (SA)
Heartbeat starts; in the right atrium where a group of pacemaker cells live
- Pacemaker cells fire off electrical signals that instruct the heart to contract 60-100 times/min
- send action potentials to the atria, causing it to contract & push blood into ventricles
- cardiac muscle fibers in atria contract simultaneously due to gap junctions
What does muscle contraction require
ATP –> mitochondria –> oxygen –> lungs
Hemoglobin function
Extracts air from the lungs, carries it through the blood, releases it in vicinity of bodies tissues
Oxygen binding molecule inside red blood cells (erythrocytes)
- gives red blood cells and blood cells the red hue
-
Metalloprotein with 4 subunits: two alpha and two beta
- each subunit has a heme group: heterocyclic porphryn ring with iron 2+ ion in the center *****binds oxygen
- can bind 4 oxygen molecules
- each subunit has a heme group: heterocyclic porphryn ring with iron 2+ ion in the center *****binds oxygen
**Also binds CO2 on the way back to the lungs for expiration
Any red blood cell contains hundreds of millions of hemoglobin

Oxygen binding to hemoglobin is…
Cooperative: number of oxygen molecules bound to a hemoglobin molecule at any given time affects how likely it is to bind more oxygen molecules – changes conformation
- In high oxygen environments, once hemoglobin binds one it is more likely to bind more
- In low oxygen environments, the removal of one oxygen makes it more likely for a second, third, fourth to dissociate
Cooperative binding
Binding of a ligand at one site of a molecule influences binding at another site
Hemoglobin conformations
T (taut) state: low oxygen conditions, low affinity for oxygen
R (relaxed) state: when oxygen binds, switches to have high affinity for oxygen
- results in oxygen binding by hemoglobin being favored when large amounts present like in lungs
- disassociation when low amounts like in tissues
Hemoglobin Oxygen Dissociation Curve
Sigmoidal shape due to cooperative binding
- low oxygen concentrations (like exercising tissues), oxygen dissociates from hemoglobin & adopts T state
- at higher concentrations, loads up on as much oxygen as possible –> R state
Curve affected by chemical environment:
- exercise causes production of CO2 and lactic acid, making blood more acidic
- also generating a lot of heat
- causes curve to shift to down and to the right
- __oxygen bonded less well, more free to dissociate into tissues
- high 2,3-BPG = byproduct of glycolysis
- curve for fetal hemoglobin shifted left, higher affinity and can steal hemoglobin from maternal circulation

Sickle cell anemia
Sickle cell trait
If just one specific amino acid in hemoglobin protein is mutated from glutamate to valine –> hemoglobin aggregates in low oxygen environment
- causes red blood cells to adopt a sickle shape
- Misshapen red blood cells can clog capillaries and become destroyed more easily - life threatening condition
Those with one copy of mutation instead of two have sickle cell trait, milder form of disease which can confer protection against malaria
Myoglobin
Oxygen storing in muscle
- only one subunit
- no cooperative binding
Higher affinity for oxygen than hemoglobin – steals oxygen from hemoglobin
Iron in myoglobin gives meat it red hue
Enteric nervous system
Nervous system dedicated entirely to function of digestive system

Salivary amylase
Lingual lipase
Lysozyme
Salivary anylase breaks down starch into smaller oligosaccharides and disaccharides (why starchy foods taste sweet if on your tongue long enough)
Lingual lipase begins process of digesting lipids (fats)
Lysozyme is an antimicrobial enzyme strong enough to kill off some bacteria
Gastrointestinal tract - following food from mouth to stomach
Highly specialized to extract nutrients - receives help from gut bacteria and enteric nervous system
Three major biomolecules - carbohydrates, proteins, lipids
- Before food hits tongue, salivary glands produce enzyme rich saliva (also lubricates food)
- enzymes digest carbohydrates and lipids (not proteins), antimicrobial
- Bolus (food) proceeds down esophagus by peristalsis
- Bolus is emptied into the stomach, passing through the lower esophageal sphincter (cardiac sphincter)
- bolus is digested into chyme: acidic mixture of semi-digested food and gastric juices
- chyme passes through pyloric sphinctor into the small intestine
Esophagus
Fibromuscular tube through which food passes to the stomach
- runs behind trachea and pierces through diaphragm en route to the stomach
Moves bolus downward by wave-like contractions of the smooth muscle lining, known as peristalsis
- can eat if upside down
Epiglottis
Flap of cartiledge that covers the trachea during swallowing to prevent food from traveling down the wrong pipe
Lower esophageal sphincter (cardiac sphincter)
Gate through which food can pass from eosphagus to stomach, but blocks contents of stomach from passing back up into the esophagus
except for Gastroesophageal Reflux Disease (GERD): caused by acidic contents of stomach escaping into esophagus when lower sphincter is weakened
Stomach
pH?
Secretions?
What can the stomach absorb?
Highly acidic chamber (great for breaking down macromolecules)
Parietal cells of the stomach secrete gastric acid: composed of hydrochloric acid and various salts
- keeps stomach pH between 1.5 and 3.5
Chief cells secrete inactive pepsin-precursor (zymogen) called pepsinogen, cleaved in acidic conditions to enzyme pepsin, which does most of protein digestion
Stomach also produces intrinsic factor: necessary to absorb vitamin B12; and water to dilute the bolus
Stomach can absorb water and certain drugs like aspirin, caffeine, small amounts of alcohol

Zymogen
Inactive precursor to enzymes
Benefits of acid in stomach
Helps with biomolecules digestion (HCl activates pepsinogen)
Neutralizes bacteria (not H. pylori)
How does stomach protect itself from acidic conditions?
Mucous epithelial cells produce bicarbonate rich mucous that neutralizes gastric acid at the lining of the stomach, providing protection
H. pylori
Bacteria in ~half of the world’s stomachs which fluorish in it’s acidic environment
- most people never experience symptoms but in some, bacteria can erode the lining of the stomach and cause painful peptic ulcers
Pylori comes from being located in the bottom of the stomach (the pylorus)
Gastrointestinal tract- stomach to large intestine
- Chyme exits stomach through pyloric sphinctor into the small intestine
- food contents move through small intestine by peristalsis- waves of smooth muscle contraction just like in esophagus
- Once food reaches duodenum, triggers release of hormones that promote digestion
- secretin: stimulates secretion of bicarbonate which quickly neutralizes acidic chyme (pH 6-7)
- CCK: stimulates release of digestive enzymes from pancreas and bile from gallbladder
- Receives response in form of digestive enzymes from pancreas and bile from the gallbladder
- brush border enzymes also aid
- Once carbohydrates, lipids, proteins all digested into smallest units: monosaccharides, fatty acids, and amino acids absorbed by epithelial lining cells
- Enter the circulatory system (fats take different route there by lymphatic system)
- Any remaining undigested material passes to large intestine where it is converted to feces
-
Feces primarily contain water and indigestible material (cellulose from plants; humans lack enzymes to digest)
- reason celery is low calory, can’t derive energy
-
Feces primarily contain water and indigestible material (cellulose from plants; humans lack enzymes to digest)
Small intestine brush border
Moves food through it via peristalsis
- invaginates in a series of folds that are composed of microscopic villi that project into the lumen
Enterocytes: intestinal epithelial cells that line the intestines
- each enterocyte has hundreds of finger-like extensions of plasma membrane called microvilli
- Greatly increase absorptive surface area (6 ft2 –>2700 ft2)
- secrete brush border enzymes: disaccharidases and peptidases
Small intestine is partitioned into
- Duodenum
- Jejunum (longer)
- Ileum
Dow Jones Industrial
Gallbladder
Gallstones- accumulate in painful fashion in gallbladder
Located just below the liver, gallbladder is small sac that stores bile produced in the liver
Bile
Yellow-green fluid produced in the liver that contains bile salts which facilitate fat absorption
Amphipathic- contain polar and nonpolar regions; nonpolar regions associate with triglycerides and polar regions associate with water on outside
- Forms spherical micelles that emulsify lipids in an aqueous environment
- lipid emulsification: breaks up lipids, exposing surface area to water soluble lipase enzymes
- also facilitates absorption by enterocytes in small intestine
Bile salts themselves aren’t enzymes

Liver functions (5)
- capillaries of small intestine drain into the hepatic portal vein which enters hepatic portal system of liver
- pick up nutrients and drugs from digestive organs and are sent to second capillary system in liver for processing
- Secretes bile
- Detoxifies compounds
- Metabolizes drugs and medications
- Stores glycogen and triglycerides
- Mobilizes glucose and fatty acids
Portal system
System of blood vessels with capillary bed at each end
- ex. hepatic portal system for liver, hypophyseal portal system in hypothalamus
Pancreas
In response to hormonal signals from small intestine, pancreas secretes an alkaline fluid containing digestive enzymes into pancreatic duct: drains into duodenum
- Enzymes include:
- pancreatic amylase: digests sugars into disaccharides
- pancreatic lipase: digests triglycerides into fatty acids and monoglycerides
- various proteases that digest proteins into amino acids and small peptides
- enzymes work best at alkaline pH
Pancreas dual function
Pancreas has exocrine and endocrine function
- Exocrine: secretes enzymes through pancreatic duct
- Endocrine: releases hormones into bloodstream
Large intestine subdivisions
-
Cecum: pouch connected to ileum of small intestine via iliocecal sphincter
- appendix: atttached to cecum; vestigial organ (serves no purpose)(may be a reservoir for healthy gut bacteria)
-
Colon: longest segment that goes over small intestine
- ascending colon
- transverse colon
- descending colon
- sigmoid colon
-
Rectum
- stores feces prior to excretion past anal sphinctor and to the anus

Large intestine main function
Absorb water from chyme converting it into solid feces
- Nutrient absorption is limited
-
Gut flora/microbiota: hosts the largest community of bacteria in human body
- synthesize necessary vitamins B7 (biotin) and K (blood coagulation) which are absorbed
Laxatives interfere with water absorption in large intestine without affecting nutrient absorption in small intestine
- ease constipation but not good for weight loss
Feces pathology
Liver dysfunction: affect bile production and lipid digestion, more fat excreted in feces = steatorrhea
Endocrine hormones that regulate digestion affect…
Affect appetite
Stimulate digestion
Halts digestion
Endocrine appetite hormones
-
leptin- hormone secreted by fat cells (adipocytes) that helps suppress appetite (feelings of fullness)
- failed to live up to hype in pharmaceutical world
-
ghrelin- secreted by specialized cells in pancreas and upper stomach when stomach is empty; increases appetite
- hunger hormone, “grrrrelin”
- gastric bypass surgery removes many of these upper stomach cells
CCK can also inhibit appetite
Endocrine digestion stimulation hormones
Digestion stimulated by signals indicated food has been ingested
- in stomach, G cells secrete gastrin: tells parietal cells when to produce HCl and intrinsic factor (gastric acid)
When acidic chyme reaches duodenom of small intestine, S cells release secretin: stimulates release of bicarbonate to neutralize chyme
Cholecystokinin also released from small intestine stimulates excretion of digestive enzymes from pancreas and bile from gallbladder
- inhibits appetite
Endocrine hormones that halt digestion
-
Somatostatin: halts pro-digestion hormones- gastrin, secretin, CCK
- also stalls stomach emptying and halts release of pancreatic insulin and glucagon
- also inhibits growth hormone release
- also stalls stomach emptying and halts release of pancreatic insulin and glucagon
Empty stomach promotes appetite, inhibits digestion
Full stomach inhibits appetite and stimulates digestion
- stomach acid and pancreatic secretion are stimulated
Enteric Nervous System “Second Brain”
Considered a branch of autonomic nervous system, not under conscious control
- other branches of autonomic also have implications on digestive tract
- sympathetic “fight or flight” contracts blood vessels to GI to direct them to muscles
- parasympathetic dilate blood vessels to GI tract to promote digestive system
Why does your body need to digest lipids
Amino acids
Carbohydrates
Maintain cellular membranes, energy storage
Synthesize new proteins
Primary source of energy
Sequential digestion of carbohydrates
- Salivary amylase breaks starches into trisaccharides and disaccharides
- Stomach doesn’t enzymatically digest carbs but does so mechanically, increasing surface area exposed to enzymes in small intestine
- Cholecystokinin induces pancreatic digestive hormones when chyme enters duodenum
- Pancreatic amylase hydrolyzes polysaccharides into di- and tri-
- Brush border disaccharidases secreted by enterocytes in small intestine turn disaccharides into monosaccharides
- sucrase: sucrose into glucose and fructose
- maltase: maltose into two glucose
-
lactase: lactose into glucose and galactose
- individuals deficient for lactase can’t digest lactose from milk/dairy
- indigested lactose passes to large intestine and fermented by bacteria –> results in gas (bloating, discomfort, flatulence)
Lactose intolerance in the world
Most of the world adults stop expressing lactase, incapable of digesting lactose
- Lactose tolerance thought to have evolved due to mutation thousands of years ago, strong selective advantage
- Mostly european ancestry
Uptake of glucose after breakdown
Intestinal epithelial cells take up monosaccharides like glucose for passage into bloodstream (Glucose= 80% of monosaccharides)
Sodium-potassium pump uses ATP to pump 3 sodium out of cell into bloodstream, 2 potassium into cell
- creates electrochemical gradient, sodium can passivly flow back into cell from _intestinal lumen v_ia sodium-glucose symporter
- lets one glucose tag along for every 2 Na into cell
- Glucose then travels via facilitated diffusion through a glucose uniporter out of cell into circulatory system
Secondary active transport: Na+ glucose symporter relies on active transport from sodium potassium pump to create concentration gradient
Uptake of galactose and fructose into bloodstream
Cellulose and other undigested starches
Galactose has similar method to glucose absorption (secondary active transport)
Fructose by facilitated diffusion
Cellulose and other undigested starches travel to large intestine and metabolized by gut flora
Digestion of proteins
Isn’t digested until the stomach, where stomach acid cleaves pepsinogen into enzymatically active form pepsin, which hydrolyzes peptide bonds in proteins
- **targets sites between hydrophobic or aromatic amino acids
- doesn’t completely break down to amino acid level
Pancreatic enzymes induced by cholecystokinin hormone triggered by acidic chyme in duodenum (small intestine)
-
trypsinogen cleaved by enteropeptidase into active form, trypsin
- trypsin: cleaves peptide bonds adjacent to lysine and arginine residue which activates suite of proteases
- ** Enzymatic regulation avoids premature activation of proteases
- if prematurely activated, digest/damage the pancrease = pancreatitis
- ** Enzymatic regulation avoids premature activation of proteases
Zymogen
Inactive precursor molecule
Uptake of amino acids after breakdown
Like glucose, aminos absorbed by intestinal lumen cells via secondary active transport
- cotransport with sodium ions following concentration gradient established by Na-K pump
- exits cell via facilitated diffusion into bloodstream
Why is uptake of amino acids and sugars similar
Both use secondary active transport with sodium potassium pump
**Monomeric sugars and aminos more or less hydrophilic, readily dissolve in aqueous environment of intestinal lumen
- lipids are hydrophobic, not readily dissolvable
Lipid absorption in small intestine
Dietary lipids are triglycerides, must be processed into fatty acid and monoglyceride components by lipase enzymes
- occurs to minimal extent in oral cavity by lingual lipase, more so in small intestine by pancreatic lipase
Spherical micelles created by amphipathic bile salts easily diffuse through plasma membrane of intestinal epithelial cells due to hydrophobic components
- In cytoplasm, fatty acids reform with monoglycerides to form triglycerides which are packaged into chylomicrons
- instead of diffuse into bloodstream, chylomicrons diffuse into lacteals:
- small lymphatic vessels that drain into larger lyymphatic vessels before going in circulation
- instead of diffuse into bloodstream, chylomicrons diffuse into lacteals:
Digestion efficiency
Extraction of macromolecules occurs hours after consumption
- 1.5L of saliva, 2 L of pancreatic solutions a day
Vitamins
Organic molecules with lots of carbon-hydrogen bonds
Often serve as coenzymes for essential processes
- ex. vitamin K a coenzyme in blood clotting
Fat soluble vitamins
Water soluble vitamins
Vitamin A, D, E, K
- accumulate in adipose (fat tissue)
- too much can result in consequences
- excess vitamin A from carrots cause turn skin orange from buildup in subcutaneous(under skin) fat
Vitamins B, C (a couple B vitamins stored in liver)
- circulate in the blood and are easily excreted
- almost impossible to take too much
Vitamin A
Retinal and retinol
- essential for vision
- interacts with opsin to form rhodopsin, which is present in the rods of the retina
- Used for low light vision
Fat soluble
Vitamin D
Acts as a hormone that regulates calcium and phosphate concentrations in the blood stream (increases absorption in small intestine)
- can be synthesized in the skin from exposure to UV radiation
- two major forms converted to active form calcitriol
Fat soluble
Vitamin K
Synthesized by bacteria in the large intestine
Essential for blood coagulation
Fat soluble
Deficiency in Vitamin C (ascorbic acid)
Common with sailors, no fresh food
- scurvy: weakness, gum disease, excess bleeding, death
Vitamin C required for collagen synthesis
Minerals
Inorganic substances required but not synthesized by the body; must be obtained in diet
- like metal ions
Macrominerals: required in significant amounts; Calcium, sodium, potassium
Trace minerals: iron, zinc, copper
Cofactors in vital processes: calcium in muscle contraction, zinc in DNA and protein synthesis
Thermodynamics definition
Heat vs. temperature
Study of heat
Temperature: measure of hotness proportional to kinetic energy
- high temp means on avg molecules are moving rapidly
Heat: transfer of energy between two objects with a temperature difference (trying to reach an equilibrium)
- when boiling water, imparting kinetic energy to its molecules and since temp is proportional its temp rises also
- increases speed of water molecules until they overcome intermolecular interactions
Kinetic energy of Ideal Gases equation
KEparticle = 1/2 mparticle vrms2
- root mean square velocity = √ 3RT / Mm
- R = Ideal gas constant
- Mm = molar mass
- T = temp (kelvin)
Temp and KE related
Fahrenheit scale points of water
Freezing point of water: 32 deg
Boiling point: 212 deg
Celsius scale
Freezing pt of water = 0 deg, boiling point = 100 deg
Body temp is 37 deg
Converting between Celsius and Fahrenheit
Kelvin to Celsius
- C = (F - 32) x 5/9
- F = (C x 9/5) + 32
- K = C + 273.15
- C = K - 273.15
Kelvin
0 = absolute temperature: lowest possible temp where motion ceases
- celsius absolute temp = -273.15 C
*** most thermodynamic equations use Kelvin but may give you Celsius, must be able to convert
Heat
Types of heat transfer (3)
Thermal energy transferred between two substances at different temperatures
- energy = Joules (kg x m2/ s2)
1. Conduction
2. Convection
3. Radiation
Conduction
Transfer of heat/kinetic energy via direct contact
- occurs across all phases of matter
- metals are excellent conductors due to delocalized electrons
- insulators don’t conduct heat well
Convection
Conduction with movement; direct transfer of KE from one substance to another
- however, focuses on circulations of fluids (gas or liquid)
Air that is heated will expand and rise and be replaced by cooler contracting air; supply of heat constantly being replenished
Radiation
Does not require direct contact between substances
Energy is transferred via electromagnetic waves
- **electromagnetic waves are produced by all objects and carry a certain amount of energy
- sunlight, heat from a fire, light bulb, thermal energy from bodies
Expansion due to heat
- When a substance heats up, molecular motion and separation increases
- substance generally expands, density decreases
- ice is less dense due to unique configuration of crystal structure of ice
-
Linear expansion: solid or liquid expands in length
- ∆L = aLL∆T
- a is coefficient of thermal expansion
-
Linear expansion: solid or liquid expands in length
-
Volume expansion:
- ∆V = avV∆T
-
Volume expansion:
Work done on a gas expanding or compressing
Pressure equation
W = - P∆ V (J)
P = F / A
Work is negative when
Work is positive when
It is being done by the system (gas) on the environment
- energy is being lost to environment
Being done on the system (gas) by the environment
- system is gaining energy
Pressure volume graph

Laws of Thermodynamics
0. Zeroth Law: If state A is in thermal equilibrium with states B and C, then states B and C must be in thermal equilibrium with each other
1. Law of conservation of energy: energy can neither be created or destroyed
- can be transformed or move with the system (universe, only truly isolated system)
2. ∆Suniverse ≥ 0
- The entropy of a system will naturally increase over time
3. At absolute temperature (0 K) a pure crystal has no entropy
1st law of thermodynamics
Conservation of energy: energy can neither be created nor destroyed, only transformed or moved
In Closed Systems:
∆U = Q - W
- change in internal energy = heat transfer into system - work performed by the system
- if system performs work, loses energy to environment
- positive value if work is done on the system
Doesn’t apply in open systems
Entropy (S)
energy not available to do work
- greater number of possible molecular configurations, the greater the entropy
- liquid has greater entropy than solid
- greater number of molecules generally means greater entropy
Change in entropy for a reversible process: ∆S = Q / T
Entropy can decrease but it requires energy
2nd law of thermodynamics
2. ∆Suniverse ≥ 0
- The entropy of a system will naturally increase over time
- entropy (S) = energy not available to do work
- If two objects are in contact but not thermal equilibrium, heat energy will spontaneously go from higher to lower temp
Entropy can decrease but it requires input of energy, however entropy of surroundings increase more so entropy of universe increases
Energy (U) is defined as
the ability to do work
Calorimetry
Calorimetry mimics combustion, which is how our body processes nutritional calories
- molecules consumed in presence of oxygen, producing water and CO2
- derives energy
Heat can be measured in Joules or Calories (not the nutritional calorie)
- 1 cal = 4.184 J
Types of calorimeters
Calorimeter- measures heat energy produced by burning a substance
- by using change of temp of water
-
Q = mc∆T
- m = mass of water
- c = specific heat capacity of water
Bomb calorimeter
Coffee cup calorimeter
Heat can be measured in…
Joules
1 cal = 4.184 J
1 Cal = 1000 cal (1 kcal) = nutritional value
A calorie is defined as
The amount of energy required to raise the temp of 1 gram of water by 1 deg C
Specific heat capacity and equation
Specific heat capacity (c): energy required to raise heat of 1 gram of substance by 1 deg C
Q = mc∆T
c of water = 4.186 J/g x C or 1 cal/g x C
Enthalpy (H)
equation
Enthalpy (H): total heat in a thermodynamic system in Joules
- ∆H = ∆U + P∆V
U =internal energy
P∆V = W –> ∆H = ∆U + W Q = ∆U + W –> ∆H = Q
- ∆H is equal to heat lost or gained in a system
Endothermic process (enthalpy)
Exothermic process
Heat is added to a system, ∆H > 0
- much of the heat put into an endothermic rxn is used to break bonds and enable the chemical rxn
Heat is removed from a system, ∆H < 0
Standard enthalpy (∆H°)
Standard enthalpy of formation (∆Hf)
∆H° = enthalpy change under standard conditions
standard conditions = 1 atm, 25 deg C
The enthalpy change associated with forming one mole of a compound from its elements under standard conditions
- element + element = compound (1 mole)
- standard enthalpy of any element in standard state is 0
- ∆Hf of O2 = 0
Standard enthalpy of reaction
∆H° of rxn = Σ∆H° of products - Σ∆H° of reactants
Given enthalpy values of reactants/products in J/mol, must factor in the amount of each compound
Use rounding and estimation

Bond dissociation energy (enthalpy)
Enthalpy change associated with breaking bonds
∆H°reaction = ∆H°bonds broken (reactants) - ∆H°bonds formed (products)
Opposite of standard enthalpy of reaction
- Forming bonds = exothermic, more stable/less energy after
- breaking bonds = endothermic
Will be given values for single bonds, double bonds, etc
Hess’s Law (total enthalpy)
∆Hrxn = ∆H1 + ∆H2 + ∆H3…
Each step must be ordered in the proper direction; reverse the sign when reversing the order of a component step, and multiply by number of moles required
Spontaneous reaction
Nonspontaneous reaction
Will proceed spontaneously on its own
Requires energy input
Thermodynamics vs. Kinetics: spontaneity unrelated to reaction rate
Gibbs free energy (∆G)
Activation energy (Ea)
Energy that can be used to perform work in a reversible reaction
- only accounts for starting state of reactants and final of products
- if free energy decreases and products are lower energy/more stable, reaction wants to occur
- ∆G < 0 , reaction spontaneous = exergonic
-
- ∆G > 0 is nonspontaneous, endergonic
- if free energy decreases and products are lower energy/more stable, reaction wants to occur
∆Grxn = products - reactants

What determines free energy state of a system (Gibbs free energy, G)
Enthalpy, entropy, and temperature
∆G = ∆H - T ∆S
T is in Kelvin ** almost always
Conditions for spontaneity (-∆G) : see picture

Thermodynamics vs. Kinetics
Thermodynamics: Stability of products/reacts, spontaneity, and equilibrium
Kinetics: rate of reaction, activation energy, rxn mechanisms
Spontaneity UNRELATED to rate of reaction
Equillibrium constant (equation)
Rateforward = Ratereverse at equilibrium
Keq = [products]x / [reactants]y
- raised to coefficients in balanced equation
**tells us the tendency of rxn to progress one way or the other
- concentrations at equilibrium, changes at different temps
**If Keq > 1, products are favored over reactants and ∆G is negative = spontaenous in forward direction
**If Keq < 1, reactants favored and ∆G > 0, non spontaneous
**If Keq = 1, ∆G = 0 and reaction is in equilibrium
******can’t use gases or solids, no H2O
∆G = -RT ln Keq

∆G under non standard conditions (not 1 atm, 25 deg C, 1 mole)
∆G = ∆G° + RT ln Q
Keq = [C]c [D]d / [A]a [B]b at equilibrium
Q = [C]c [D]d / [A]a [B]b at any point in rxn
- if Q > Keq, products higher than at equilibrium and goes in reverse
- when Q < Keq, reactants move in forward direction
- when Q = 0, equilibrium
Catalysts
Needed when a reaction can’t surpass activation barrier on its own
- Enzymes
- increases rate by lowering activation energy in both directions
Protein folding refers to…
Globular proteins
- Spherical
- myoglobin
- Serve functional roles
- enzymes, peptide hormones, regulatory molecules
- Generally water soluble
- Spherical
Types of proteins
Globular- spherical, water soluble, serve function, protein folding
Fibrous- elongated (sheet-like), hydrophobic, ex. collagen
Membrane proteins- attached to plasma membrane
Why does protein folding occur (tertiary structure)
- Entropy- increase in entropy is favorable
- Folded protein has lower entropy than unfolded, however, hydrophilic solvents lose entropy when they form solvation layer arond hydrophobic side chains
- protein folding conceals hydrophobic side chains
- minimal contact with hydrophobic side chains = maximum entropy
** protein folding driven by hydrophobic interactions, cluster together to avoid hydrophilic groups/molecules
** Hydrophobic core (nonpolar aminos), hydrophilic shell (polar aminos)
solvent molecules free to interact with polar aminos, increases entropy=favorable

Protein denaturation
Loss of non-primary protein structure
- does not break up primary structure!!! unfolded chain of aminos
Primary structure much harder to disrupt than higher-level structure
- Held together by peptide bonds which are covalent bonds between nitrogen and carbon atoms
-
intramolecular bonds stronger than intermolecular forces
- sec structure = H-bonds, tert/quat = non-covalent side chain interactions, disulfide bonding
-
intramolecular bonds stronger than intermolecular forces

Denaturing Agents (proteins)
Temperature extremes
- high temp disrupts non primary interactions, can render protein non-functional
- low temp can decrease protein/enzyme activity, decrease in collisions
- human proteins optimized for body temp
pH extremes
- disrupt charge based interactions in tert/quat structure
- salt bridges form due to ions opposite charges, high or low H+/OH- conc in pH can change these
Detergents (like soaps)
- part polar/part nonpolar disrupts hydrophobic interactions
- SDS used in SDS-page
Reducing agents
- disrupts covalent bonds b/w sulfur atoms (disulfide bonds) via reduction, reforms SH group
Specific compounds
Heat- irreversible
Urea- reversible when urea is gone
What is capable of breaking protein primary structure
Protease enzymes
- catalyze hydrolysis of peptide bonds
Often grouped by catalytic mechanism
Favor cleavage at specific sites on target protein - like trypsin
- aminopeptidases cleave from N-terminal
- carboxypeptidases cleave at C-terminal
Flow of electrons
Electrons flow from electron rich areas (like oxygen in H2O) to electron poor areas, driven by their physical properties
- electrostatic attraction between pos and neg and repulsion between neg and neg
Electron rich = nucleophile, electron poor = electrophile
Electrophile
Electrophile: short on electrons, wants more
- positive or partial positive charge
strong electrophile really wants more, positive charge or empty orbital
- __carbocations or hydrogen ions, aluminum chlroide (AlCl3) is neutral with empty orbital
weak electrophile has partial positive charge, generally due to induction of more electronegative atoms
- carbonyl carbon has electron density drawn away by oxygen
Electrophiles –> accept electrons –> lewis acids
Site vs. Species (electrophiles and nucleophiles)
Electrophilic or Nucleophilic site: refers to the exact location, usually an atom, that acts as electrophile or nucleophile
Electrophilic/Nucelophilic species: shorthand way of denoting which molecule has relevant electrophilic or nucleophilic site, without being overly exact
Nucleophiles
Donate a pair of electrons to another species to form a covalent bond
- has lone pairs
- pi bonds (double/triple bond) can act as nucleophile
Can be strong- negative charge
weak- neutral with lone pair or pi bond
Case to case basis, NH3 is neutral but a strong nucleophile due to hydrogens not pulling electron pair from N atom
Nucleophiles attack electrophiles, donate electrons –> lewis bases

Nucleophilic substitution
SN1 vs. SN2
Nucelophile replaces other functional group (leaving group)
SN1: Reaction rate depends on concentration of ONE reactant (the electrophile)
- Rate = k[A]
SN2: Reaction rate depends on both reactants
- Rate = k[A][B]
Nucleophilic substitution
SN1
Two steps:
- Leaving group leaves, generates carbocation (slow)
- carbocation formation = rate limiting step
- depends only on concentration of substrate, reason rxn rate only depends on electrophile
- carbocation formation = rate limiting step
- Nucleophile attacks
- often molecule of water or alcohol, will become positive
- next step is to deprotonate
Not stereosensitive, can attack from front or back –> equal conc of S and R enantiomers
- Racemic mixture of products
Good vs. bad leaving groups
Good leaving group:
- stable in solution after leaving – does not promote reverse rxn
- like water in aqueous soln
- also has positive charge which helps it leave (OH2+)
- many times want to protonate hydroxyl
-
halogens:
- I > Br > Cl > F
- like water in aqueous soln
Nucleophilic substitution: SN2
Nucleophile and electrophile involved in rate-limiting step; rxn rate depends on both their concentrations
No carbocation is formed, weaker electrophiles
- most common substrate is alkyl halide (tert, sec, or primary)
- Carbon attached to halogen has partial positive charge
- Nucleophile must attack opposite (back-side) of leaving group (halogen)
- both nucleophile and leaving group are electron rich
- substrate chirality is inverted (ex. S–> R)
Predicting SN1 reactions
Both can co-occur in same rxn, one is usually dominant
For Sn1, increased carbocation stability makes it favorable
- 3° > 2° > 1° = number of alkyl substituents, each makes carbocation more positive
- must be tert or sec for Sn1 to occur
Nucleophile strength not very important for Sn1, but solvent is important
-
polar protic solvents: polar and can form H-bonds, highly electronegative
- water, alcohols
- stabilizes carbocation and interacts with leaving group

Sn2 reaction conditions
Driving force: nucleophilic attack
- nucleophile must be strong and be able to reach electrophilic carbon on substrate
- nucleophile must also be non-bulky to avoid steric contraints
- also non-bulky substrate
Reactivity order: 0’ (methyl) > 1’ > 2’ > 3’ (opposite of Sn1)
Polar aprotic solvents preferred: polar but lacks acidic hydrogens (can have other hydrogens)
- acetone and DMSO, don’t affect nucleophilicity like protic solvents

Hydrolysis
How peptide bonds are broken down; nucleophilic substitution rxn
- water is nucleophile to cleave bonds, inserts itself
Opposite is dehydration-condensation rxn
Also the reverse of fischer esterification

Fischer esterification
Acid catalyzed subsitution rxn that takes place at carbonyl carbon
- carboxylic acid into an ester
- OH group is replaced by OR group which is an alcohol
- Takes place in presence of strong acid like HCl or H2SO4
*Can be reversed = hydrolysis
Don’t need to memorize
- Acid protonates carbonyl oxygen, resonates and makes carbonyl carbon more electrophilic
- Alcohol acts as nucleophile and forms tetrahedral intermediate
- Goal is to eleminate either one of hydroxyl groups, which must be protonated first by acid presence
- Other hydroxyl reforms carbonyl with its H+, kicking off H2O+
- Deprotonation

Imine formation
Substitution rxn: electrophilic substrate must have carbonyl carbon NOT part of carboxylic acid group
- commonly ketones
Nucleophile is an amine (contains N with lone pair)
- Acid catalyzed, carbonyl oxygen replaced by nitrogen (C to N double bond)
- similar to Fischer esterification

Elimination reaction
E1
E2
(not heavily tested)
Leaving group leaves without nucleophilic addition
- new C=C double bond forms
E1: 2 steps, Rate = k[A]
- carbocation formation, alkyl halides
- Bronsted lowry base (proton acceptor) pulls off H from carbon and leaving group leaves
- leaves behind electron pair which forms double bond
- Can be weak base
E2: 1 step, Rate = k[A][B]
- Base attacks hydrogen adjacent to carbon of leaving group, crashes down to form double bond
- kicks off leaving group
- Requires strong base

Nucleophilic addition
Nucleophile just adds itself to compound, no leaving group
Requires electrophile with double or triple bond: carbonyl, nitrile, alkene, alkyne
- Focus on alcohol attacking aldehyde or ketone forming hemiacetal or hemiketal
- can be catalyzed by either acid or base
- Tetrahedral intermediate is stable
Acid catalyzed: strong acid protonates carbonyl oxygen making electrophile stronger, then alcohol attacks carbonyl carbon
Base catalyzed: nucleophile made stronger by deprotonation (strong base deprotonates alcohol), attacks electrophile
- if too much alcohol conc, another can attack and form an acetal/ketal
Why is nucleophilic addition important
Drives cyclization of monosaccharides from linear form
- alcohol group on linear chain attacks carbonyl carbon of ketone or aldehyde
When two sugars come together to form a disaccharide, glycosidic bond forms between them
Tautomerism
Tautomers: two structures of a molecule that can easily interconvert at equilibrium
Does not equal resonance (electron delocalization)
Tautomers entirely different and interconvert by breaking/forming bonds
- aldehyde or ketone and enol interconvert; enol (ene and ol) has C=C double bond and -OH group
Enamines and imines
Amides and imidic acids
Keto-enol tautomerism
Ketone/aldehyde interconvert with enol (-ene and ol, C=C and OH group)
- different mechanisms for acidic and basic conditions
Both must have one acidic alpha hydrogen that can be removed by a base
- alpha hydrogen: any hydrogen connected to a-carbon (carbon next to carbonyl carbon)
With asymmetric ketones, there can be multiple products where double bond forms – depending on thermodynamic vs. kinetic
Acid catalyzed keto-enol tautomerism
Starting w/ acetone = ketone
- Strong acid like H2SO4 protonated carbonyl oxygen
- goal is to remove positive charge this creates on the O
- H2O acts as weak base and removes one acidic a-hydrogen
- electrons in its bond stay behind, form a double bond with carbonyl carbon
- Carbonyl double bond pushes up lone pair two oxygen, which now has two lone pairs
- goal is to remove positive charge this creates on the O
Base catalyzed keto-enol tautomerism
Starting with acetone ketone and NaOH strong base
- Base can attack a-hydrogen directly, forming double bond with carbonyl carbon and a-carbon
- puts negative charge on carbonyl oxygen, which picks up proton from water molecule formed in first step
Base OH is not consumed, only participates

Enol stability
in aqueous soln, 99% keto and 1% enol
- Factors that can stabilize enol form:
-
resonance: phenol is aromatic, more stable than keto form
- H-bonding: protic solvent can stabilize enol form
-
resonance: phenol is aromatic, more stable than keto form
Resonance of enolates
Enolate anion created as intermediate in base-catalized keto-enol tautomerism
- negative charge on carbonyl oxygen can shift to a-carbon
- Enolates can act as nucleophiles; carbon acts as nucleophile
** rarely see negative charge on carbon

Kinetic vs. thermodynamic enolates
Kinetic
- formed most quickly; less stable long term
- Rapid, irreversible
- Low temperature
- strong bulky base
- double bond forms at less substituted a-carbon because less hindered
Thermodynamic
- double bond b/w carbonyl carbon and more substituted a-carbon
- form less quickly, more stable long-term
- high temp
- weaker, less hindered base
Aldol Condensation
Two molecules of aldehyde or ketone condense through nucleophilic attack to form an aldol: aldehyde or ketone and alcohol
- can be under acidic or basic conditions, basic is more common
- ** aldehydes and ketones can act as nucleophiles and electrophiles
Cross Aldol condensation: between two diff aldehydes or ketones, or an aldehyde and ketone – unpredictable and tons of products
Many different products
***Alpha beta unsaturated products suggest aldol condensation
*** number carbons when asked for major product
*** can happen backwards

Base-catalyzed aldol condensation
- Strong base removes alpha hydrogen –> enolate
- Enolate attacks carbonyl carbon of another aldehyde which forms C-C bond
- Neg charge on oxygen product gets protonated and forms aldol
In many reactions, aldol isn’t final product
- Spontaneous dehydration can removes OH group
- base removes a-hydrogen from same a-carbon causing double bond b/w a-carbon and carbon with hydroxyl group, kicking it off
- Forms a,B-unsaturated aldehyde
Acid catalyzed aldol condensation
- Enol formed through keto-enol tautomerism
- C=C bond in enol used as nucleophile
- Second aldehyde prepared to be electrophile by protonating its carbonyl oxygen
- Enol double bond attacks electrophile carbonyl carbon, forms bond b/w a-carbon of enol and carbonyl carbon of electrophile
- forms aldol
usually is then changed into a,B-unsaturated aldehydes

Michael addition
Aldol condensation can give rise to a,B-unsaturated products
- name implies double bond between a and B carbons adjacent to carbonyl carbon
- nucleophiles can add to carbonyl carbon AND beta carbon due to resonance
- Michael addition: enolate attacks BETA carbon
- alpha carbon is protonated
- Results in two carbonyls separated by 3 carbons

Robsinson annulation
Michael addition followed by aldol condensation
- strong base forms enolate by pulling a-hydrogen from a-carbon
- Negative alpha carbon nucleophilic attack at other carbonyl
- forms cyclic structure
- Aldol condensation dehydration rxn pushes off OH via elimination which forms new C=C double bond
Forms six membered ring with applications in synthesizing steroid hormones and certain drugs
Coulomb (C) unit definition
Coulomb’s Law
amount of charge carried by a current 1 ampere in 1 second (A x s)
- elementary unit of charge = e :
- charge of proton and electron = +- 1.602 x 10-19 C
Coulombs law: calculates force charges exert on eachother
- F = k (Qq / r2)
- q is test charge, Q is source charge (helps for thinking about electric fields)
- r = distance b/w charges
- k = coulombs constant
**attractive forces decrease with the square of distance
mass
quantitative measure of inertia, a fundamental property of all matter. It is, in effect, the resistance that a body of matter offers to a change in its speed or position upon the application of a force
weight = mg
m = density x volume
F = ma
Resistivity and Conductivity
High resistivity (low conductivity): charge doesn’t readily flow through substance (high þ)
- insulators
High conductivity: charge readily flows (high σ)
- Conductors
- favor conduction: large area, short length
- resistivity and conductivity are a spectrum
Opposite charges attract, like charges repel (pos and neg)
Electric Field
Any single point charge can exert a force on any other single point charge
magnitude of an electric field =
- force experienced by charge / magnitude of charge
-
E = F/q
-
- q = test charge, charged particle used to test magnitude of field at any given point
E = kQ / r2 (combines coulombs law, Q = source charge)
Similar to gravitational field
- shows field strength changes with distance
Electric Field Lines
Capacitors
Arrows point in the direction that a positive test charge would travel in an electric field
- away from pos charge, toward neg charge
capacitors- linear charged plates that create an electric field between them

Torque
Force that causes rotation
T = Fd sin (0)
Electrical work definition = electric potential energy
Electric Potential
Electric potential energy = U = kQq / r
Work is in Joules, also the unit for energy
Electric potential = V (volts) = U / q = Joules / Coulombs
- q = test charge
- Volts are a measure of how much energy is needed to move a certain amount of charge to a certain point in an electric field
- if movement is spontaneous, how much energy is released
Not the same thing! electric potential normalized for charge
Equipotential lines
Voltage
Connect all points with same electric potential
- perpendicular to field lines
Voltage: Electric potential difference between two points on different equipotential lines
- ∆V = ∆U / q
No work done by or against an electric field when moving charged particle along equipotential line

Magnetism
Diamagnetic, paramagnetic, ferromagnetic
Produced by the spin of elementary particles (electrons)
- electrons have spin of +1/2 and -1/2
- magnetic dipole moments that cancel out in full orbitals
-
diamagnetism: **materials with only paired electrons do not generate a magnetic field
- water, wood, fabric
- weakly repelled by magnets
Paramagnetic: unpaired electrons have random spins, material as whole have no net dipole
- weakly attracted by magnetic fields
- external field can temporarily fix electron spins and create magnetic polarization
Ferromagnetic: unpaired electrons have stable nonrandomized electron spin – permanent magnets
Magnetic dipoles
Basic unit of magnetism, like charge for electricity
- every magnetic dipole has a north pole and south pole
- opposites attract
- north can’t exist isolated without south, vice versa
Magnetic fields (B)
What is their unit, how do their lines run, what are some conditions
Magnetic field equation shows:
Magnetic field lines run from north to south (electric run from pos to neg)
- strength of magnetic field in Teslas (T)
-
Tesla: magnitude of magnetic field at which a particle with a charge of 1 coulomb moving perpendicularly at 1 m/s experiences force of 1 Newton
- *large unit of force
** magnetic fields only exert force on moving charges, moving charges also generate magnetic fields
Strength of magnetic field directly proportional to current, inversely (but linearly) proportional to distance from current
B = u I / 2πr (u = permeability of free space, I = current, r = distance)
Directionality of magnetic field
Direction of field around current carrying wire determined by right hand rule
- “hold” wire with right thumb pointing in direction the current is flowing and fingers curl around in direction of magnetic field
- opposite direction of electron flow
circle with X = field going into page
circle with dot = field coming out of page
(think of an arrow)

Magnetic force equation
what it implies
FB = q v B sin0
- FB = force exerted by magnetic field (vector, has magnitude & direction)
- q = charge of particle
- v = velocity (vector)
- B = strength of the magnetic field
- Theta 0 = angle of velocity of particle to magnetic field
Important: force directly proportional to charge and strength of magnetic field; if any of these values are zero, no force from magnetic field
- **For force, particle must be charged and moving and magnetic field must have strength
**Sin(0) means maximum force when moving perpendicular, 0 when moving parallel
magnetic force for current carrying wire
determining directionality of vectors
FB = I l B sin(0)
I= current in Amperes (C/s)
l = length of wire (m)
Directionality- second right hand rule

Electromagnetism (lorentz force)
A summation of the forces exerted on a charge by electric and magnetic forces
Ohm’s Law
Current =
Direct Current =
Ohms Law: V = I R
- ohms= volts / amperes
Current follows the movement of positive charge (not movement of electrons)
Current = charge/ time
- in Amperes (C/s)
Direct Current: current that moves in a single direction through a circuit
Resistance
Resistivity described by Rho (p) and conductivity described by σ, material specific constants for given temperatures
- describe degree to which physical material resists/conducts current
- inverse concepts
resistance (R) = p (l / A)
conductance (G) = σ (A / l)
- large area and short length favor conduction

Circuit components:
What makes current move?
-
Resistors: resist moving charge
- kind of like friction, allows current to be changed to heat or light
- Capacitors: store charge
- Conductive wire
What makes current move? Voltage, electric potential difference between two points that charges flow spontaneously across
- current flows from positive point of voltage to negative (current positive wants to go to negative)
*** voltage differential that powers a circuit (usually in battery) is called the electromotive force (EMF)
- Long line= +
- short line = -

Power
Power dissipated by a current
Rate at which energy is used or produced
- Power = Work/ Time (J/s)
- Power dissipated by a current = P = IV
- **can factor ohm’s law into equation V = IR
Derivation:
Volts- electric potential energy of a charge at a given point in an electric field, divided by the magnitude of that charge
- V= U / q
- Work = ∆U (change in electric potential of energy)
Activation energy (Ea)
For a reaction to take place, activation energy threshold must be overcome– Represents transition state , high energy and unstable
- Reactants –> transition state –> products
- Determines how quickly a reaction will proceed – kinetics

Chemical Kinetics refers to
For a reaction to occur:
Chemical reaction rates – controlled by activation energy and temp.
Reactants must collide with each other in specific orientation and with sufficient kinetic energy –>
- transition state: formation of unstable intermediate
How to lower Ea
Lowering Ea done by deploying catalysts (enzymes)
- stabilize transition state
- weaken bonds within reactants
- changing orientation to elicit effective collisions
- increasing frequency of collisions
- donating electron density to reactants
Enzymes don’t affect thermodynamics: Gibbs free energy, enthalpy, entropy
Catalysts not consumed, small amount can greatly affect products
Heterogenous vs. Homogenous Catalysis
Based on the phase of catalyst compared to phase of reactant species
heterogenous catalyst: in different phase than reactants
- typically catalyst is solid and reactants are liquid/gas
- based on surface area of catalyst, grinding it into a powder more efficient
homogenous catalyst: same phases
Rate of a Chemical Reaction defined as
Expressed mathematically by:
- Reaction order:
Disappearance of reactants over time/appearance of products (Molarity/sec)
- Molarity= moles/L
expressed mathematically by Rate Law: relationship b/w reactant conc. and rate of rxn
- rate= k[A]x[B]y
- where x and y denote rxn order w/ respect to A and B
-
order: degree to which rate of rxn is dependent on reactant
- sum of reactants orders give overall order (x+y)

Reaction order:
Degree to which rate of rxn is dependent on each reactant (rate = k[A]x[B]y
- overall order is sum (x+y)
Zero order = [A]0[B]0 ; rate doesn’t depend on reactants
*Rate law only includes reactants that determine rate, can be others
How to find rate law (elementary rxns, multi-step rxns)
Initial rates method
Rate constant (k)
In one step elementary rxns, coefficients of reactants are their orders
In multi-step rxns, found by slowest/rate-limiting step
- determined experimentally with trials, one Reactant conc changes while other stays the same
- compare the rate to the conc using rate equation and solve for the order (reference pic)
Units of k vary depending on overall order:
k = rate / [A]x[B]y
To find units, just plug in what you know and solve for k

How are zero order reactions possible?
What do first order reactions consist of?
Second order?
Zero order reactions: unaffected by changes in reactant concentrations
- ex. enzyme catalyzed reactions in which enzyme is saturated.
- reactant concentrations far exceed available active site
First order: radioactive decay or SN1 reactions
Second order: physical collisions between two reactant molecules
Simple circuits: how does current flow?
How is ∆V= IR applied (ohm’s law)
Current flows from high voltage to low voltage (- towards +)
- voltage drop isn’t distributed evenly across circuit
∆V = IR can be applied to circuit as a whole as well as components
- can apply to resistor(high voltage drop) and conductive wire (has no voltage drop)
Resistors in Series
Resistors in Parallel
Resistors in series: added one after another, no junctions
For a circuit with 3 resistors in series:
- Itotal = I1 = I2 = I3
-
Vtotal = v1 + v2 + v3
- ***voltage drops in circuit have opposite sign as EMF
- Rtotal = R1 + R2 + R3
Resistors in parallel: current is split, branches into different resistors
3 resistors in parallel:
- Itotal = I1 + I2 + I3
- **Vtotal = v1 + v2 + v3
- 1/Rtotal= 1/R1 + 1/R2 + 1/R3

Kirchhoff’s Laws (circuits)
-
Kirchhoff’s first law: Itotal = I1 + I2 + I<strong>3… </strong>
-
The sum of current entering a junction must equal the sum exiting the junction
- Kirchhoff’s second law: vtotal = v1 + v2 + v3
- The sum of the voltage drops throughout the circuit is equal to source voltage (EMF)
-
The sum of current entering a junction must equal the sum exiting the junction
Ammeter measures…
Voltmeter measures…
Ohmmeters measure…
Ammeter measures current (in amperes)
- inserted in series, has zero resistance
Voltmeter calculates voltage
- inserted in parallel
- has known resistance, ideally uses least amount of current possible
- since resistance added reciprocally in parallel, has little effect
Ohmmeters measure resistance
- has known resistance, uses little current
Capacitors
Devices that store electrical charge, two physically separated components where opposite charges are accumulated
- parallel, flat, thin, conductive plates separated by nonconductive insulated material (dielectric)
- accumulation of charge is due to voltage applied
*
Capacitance (C)
equation
Dielectric constant
capacitance: degree to which a capacitor can store charge
-
C = Q / V amount of charge stored given a voltage
- in farads which is 1 coulomb/ 1 volt
Depends on area of conductive plates and dielectric material (insulator between them, the better the insulator the more charge that can be builtup)
C = Σ0 (A/d)
- Σ0= permitivity of free space (in a vacuum)
- A= area (bigger area, higher C)
- d= distance b/w plates (smaller distance, higher C)
K= dielectric constant = Σm / Σ0
- every insulator has higher permitivity than Σ0 (vacuum)
- The greater K, the more charge it can store
Properties of capacitors
- Create uniform electric fields, strength of which is defined by E=v/d
-
eqn only applies to uniform fields
- Store energy in the form of the electrical field that they generate which is potential energy
- PE = 1/2 CV2
-
eqn only applies to uniform fields
- Capacitors in series add reciprocally, capacitors in parallel add directly
- __Opposite from resistors
Used for defibrillators, **electrical potential difference across cell membranes (usually -70 mv)
Reversibility in reactions
Haber Process (reversible rxn)
Reaction can progress forward and in reverse
- majority of reactions in chemistry
- irreversible only progress forward
1 N2 + 3 H2 = NH3 (ammonia)
Equilibrium
Forward and reverse reaction rates are equal
- Does not mean reactant and prodct concentrations are equal, but they are stable
THERMODYNAMICS- if spontaneous rxn, favors products and equilibrium will have higher product conc
- nonspontaneous favors reactants
at Equilibrium, entropy is maximiazed and ∆G = 0, stays at equilibrium unless disturbed

- Factors that affect equilibrium constant Keq
- Keq of reverse reaction =
- Temperature affects Keq value
* Factors that don’t: amount of concentration, presence of a catalyst (impacts kinetics) - Keq of reverse rxn is 1/Keq3.
The Reaction Quotient (Q)
Reaction quotient tells us if given concentrations are at equilibrium
- aA + bB = cC + dD
- Q = [C]c[D]d / [A]a[B]b
Shows which direction reaction proceeds toward equil
- low Q means reactants dominate mixture, high Q means products do
Must be compared to Keq
- Q < Keq : less product than it should at equilibrium, rxn goes forward
- Q > Keq : reverse direction towards reactants
- Q = Keq is at equilibrium
Le Chatelier Principle
How reaction mixtures respond when shifted from equilibrium
Stress = change in reactant/product concentration, change in temperature, pressure, volume causes a shift toward reactants (left) or towards products (right)
- If A + B = C and additional “A’ is added, reaction shifts to the right and more “C” is formed
- less B concentration at equilibrium than before
- Concentrations fix themselves proportionally to Keq value in equation
- Keq = [C]/ [A][B]
Removing product as its formed can increase reaction yield for the product
How to make the most Acetylsalicyclic acid (ASA) during synthesis
(Aspirin)
- Excess reactant (acetic anhydride) to drive rxn toward products
- Removal of product after its synthesized

What is a solution
Solutions can be…
A homogenous mixture
-
mixture: 2+ substances where substance remains its own identity
- can be homogenous- uniform composition
- or heterogenous- uneven distribution
- sand at the bottom of a glass
Solutions can be gaseous, liquid, or solid; in chemistry usually is solid molecules dissolved in liquids
Dissolution
Solvation
Dissolution: Act of dissolving
-
solute (minority compnent) is dissolved in/interacts with particles in the solvent (majority component)
- solvent separates solute molecules or breaks ionic molcules into ions
Solvation: abundant individual solvent particles surround solute particles
- like dissolves like
Saturated solution
Unsaturated solution
Supersaturated solution
Extent to which solute can be dissolved in a solvent
saturated solution: maximum amount of solute that can dissolve in given solvent has been added
- adding more solute will form a precipitate
unsaturated solution: contain less than maximum amount of solute
supersaturated solution: more than max amount of solute dissolved in solution
- higher temperature when dissolved, cool very slowly and it will remain
- crystallization: adding more solute once solution cooled, excess solute crystallizes
Solubility vs. Ionization
Solubility: the extent to which a substance dissolves in a solvent
Ionization: dissolution of ionic compounds
- Ionic compounds DO ionize when they dissolve in solution
Electrolyte
Dissolution of ions results in charged species in water
- Ions in solution conduct electricity
Effect of temperature and pressure on solubility (for gases and solids):
Temp: for solids, higher temp = higher solubility depending on if reaction is endothermic or exothermic
Gases more soluble in liquids at lower temperatures
- __Dissolved O2 content in bodies of water is higher during winter than summer
Solubility Rules (what compounds are always soluble)
**most important, “absolutes”
- **All alkali metals (Li+, Na+, K+, Rb+, Cs+, Fr+) and ammonium salts are soluble
- **All nitrates (NO3-), chlorates (ClO3-), and acetates (CH3COO-) are soluble
-
Halides (Cl-, Br-, I-) are soluble
* unless combined with lead, mercury, silver -
Sulfates (SO42-) are soluble
* except with calcium, strontium, barium, lead, silver -
Carbonate (CO32-), phosphate (PO43-), sulfide (S2-) and sulfite (SO32-) are insoluble
* except with alkali metals - Hydroxides and metal oxides are insoluble
* except with alkali metals, Ca, Sr, or Ba
Concentration in a solution can be expressed in 3 ways:
Molarity: (M) moles of solute / liter of solution (M/L)
- 1 mM = 1/1000L
Molality: (m) moles of solute / kg of solvent
- 1L of water = 1 kg
- more impact in higher solute conc (affects the volume)
Normality: (N) number equivalents of solutes per 1 liter of soln
- for acid/bases, equivalents are H+ and OH-
Colligative Properties (4)
Properties changing solely due to concentration of solute in solution
** Does not depend on identity of solute, depends on total number of dissolved solute particles
- ex. adding salt to water raises its boiling pt, lowers its freezing pt
Freezing pt depression
Vapor pressure reduction
Boiling pt elevation
Osmotic pressure
How to calculate normality (N) (in acid base context)
Normality of acid (N) = molarity of acid x number of protons per molecule
Normalitu of base (N) = molarity of base x number of hydroxide atoms
Solubility Constant (Ksp)
Ksp = [C]c[D]d / [A]a[B]b
Follows exact same rules of Keq
MgCls (s) + H2O (l) = Mg2+(aq) + 2Cl-(aq)
- Ksp = [Mg2+][Cl-]2
** high Ksp means high conc of dissolved ions compared to initial solid, high solubility
**low Ksp means low solubility of initial solid, insoluble
also a Q value for concentrations not at equilibrium

Molar solubility
Number of moles that need to dissolve for a soln to be saturated
Common Ion Effect
Solubility of an ionic species decreases when one of its component ions (common ion) is already present in solution
- the higher the conc of common ion, the less solute that can dissolve before Ksp is reached
Example of Le Chatilier Principle
AgCl —> Ag + Cl
Ksp= [Ag][Cl]
If Cl goes up, Ag goes down to equal Ksp value

Coordination Complex/ complex ion
Helpful with common ion effect
Ions can form different molecules in solution that will take away its concentration from that of the solubility Ksp equation

Acid Base chemistry and common ion effect
H+ and OH- can be common ions if present in solution with an ionic species that contains them
- the more basic a solution, the lower the solubility of a molecule like NaOH
A base added to an acidic soln ionizes more
An acid added to a basic soln ionizes more
MCAT can use wording like base or pH to imply common ion effect
- Arrhenius acid bases (earliest)
- Bronsted Lowry
- Lewis
- Arrhenius: Acids and bases dissociate to form different ions; Acids form H+, Bases form OH-
- acids must contan H+, bases must contain OH-
- *NH3 is a common base without OH group
- not very broad
2.*** Bronsted Lowry: Acid is a proton donor (loses H+), Base is a proton acceptor (gain a bond to H+)
- after acid loses its proton = conjugate base
- when base gains a proton = conjugate acid
- typically what MCAT refers to if not specified
3. Lewis: acids are electron acceptors, bases are electron donors
- most inclusive definition

Amphoteric Species
Can either accept or donate a proton (acid and base)
- water, amino acids
Acid base equilibria
Kw, Ka, Kb
Equilibria of reactions in which protons are gained/lost
- ** protons exist as H3O+ in solution (hydronium)
Kw: equilibrium for auto-ionization of water (Kw= [H3O+][OH-])
- equilibrium strongly favors reactants, H2O
- 1 x 10-14 at 25 deg C, larger at higher temp
- 1:1 ratio of H3O and OH
Ka: acid dissociation constant
- Ka = [H+][conj base]/[acid]. ** high Ka dissociates more readily
- low Ka acid dissociates less readily
Kb: base dissociation constant
- high Kb means base dissociates readily

If pH is 8 and H3O+ and OH- concentrations are equal (like water at 0 deg celsius)…
The solution is still neutral
Pure water is neutral at any temp
*** pH of 7 is only neutral at standard state temp
Acid-Base strength tells us…
Strong acid properties
How readily acid/base dissociates in reaction
-
strong acids:
- ionize fully in water
- have large Ka values
- tend to produce soln with low pH
-
strong bases:
- ionize fully in water
- large Kb values with high pH
-
strong bases:
Strong acids to memorize
HI. Hydroiodic acid
HBr. Hydrobromic acid
HCl. Hydrochloric acid
HNO3 Nitric acid
H2SO4 sulfuric acid
HClO3, HClO4. chloric acid, perchloric acid
3 M HCl = 3 M H3O+
Strong bases to memorize
Hydroxides of alkali or alkaline earth metals, like NaOH, KOH, Ca(OH)2
NH2-
H- hydride
CH3O-
CH3CH2O-
(CH3)3CO-
methoxide, ethoxide, tert-butoxide
**assume all other bases weak.
Equations
pH and pOH
pKw, pKa, pKb
“p” stands for negative log; pH = -log[H+]
pOH = -log[OH-]
pKw = -logKw = pH + pOH = 14 **at 25 deg C
- **pKa + pKb = pKw = 14
pKa = -logKa
- pKa get smaller as Ka gets bigger
pKb = -logKb
- pKb gets smaller as Kb gets bigger, stronger base
Ka x Kb = Kw
Acid and its OWN conjugate base
- If acid A > acid B, conj base A < conj base B
- acid A likes to give up proton more, will have more stable conj base (doesn’t want to pick back up proton)
Acid naming
- Named depending on if:
-
Organic: compounds with carbon-hydrogen bonds
- carboxylic acids: propanoic acid
- -oic acids
-
Inorganic: don’t contain oxygen
- like HI, HBr
-
Hydro + -ic acid
- hydroiodic acid
-
Hydro + -ic acid
- like HI, HBr
-
Oxyacids: inorganic acids with oxygen
- name depends on # of oxygen atoms
-
-ic corresponds to -ate anion
- HClO3 = chloric acid
- _+1 oxyge_n = per-
- perchlorate = perchloric acid
-
-1 oxygen = -ous
- Chlorite = chlorous acid
-
-2 oxygen = hypo- and -ous
- hypochlorite = hypochlorous acid
-
Organic: compounds with carbon-hydrogen bonds
Ate to ic
Colligative property: Vapor pressure reduction
Equation
If a liquid is exposed to air, some will evaporate into a gas until gas and liquid phases reach equilibrium; increases with temp
- pressure exerted by gas above liquid is vapor pressure
Adding solute to liquid reduces amount of gas produced
- attraction between solvent and solute particles
- surface composed of solvent and solute, less surface area for solvent to evaporate
- solutes must be nonvolatile (don’t evaporate readily)
P = XaPa
Vapor pressure in soln = mole fraction x vapor pressure of pure solvent
More solute, more VP of soln
Colligative property: Boiling point elevation
Equation
Temperature at which vapor pressure equals atmospheric pressure
Adding solute decreases VP and increases boiling pt
- doesn’t depend on type of solute, depends on number of solute particles
∆Tb = iKbm
i = ionization / Van’t hoff factor for solute (NaCl = 2)
Kb= constant for solvent
m = molal solute conc (moles solute / kg solvent)(1 for water)
Colligative property: Freezing Point Depression
equation
∆Tf = iKfm
Change is a decrease in freezing point
i = ionization factor
m= molality
Colligative property: Osmotic pressure
Pressure required to prevent osmosis: flow of solvent through a semi permeable membrane across concentration gradient, from low solute to high solute
- equalize concentrations
Osmotic pressure stops this flow to counteract osmosis
- used for biological membranes
- depends on total number of solute particles given by ionization factor (i)
π = iMRT
i x molarity x gas constant x temp
Buffer function
Equation (henderson-hasselbalch)
half equivalence point is
Solution that resists changes in pH when an acid or base is added
- created from weak acid and conjugate base or weak base and conjugate acid
- highly effective to small to moderate quantities of base or acid
pH = pKa + log10 (A- / HA)
- pH is pH of buffer and pKa is that of the weak acid
- **pKa = pH when acid is 50% protonated (half equivalence point)
- A-/HA = 1 and log101 = 0
What acid base pair is a good buffer?
Acid has a pKa close to desired pH of solution, most effective when amounts of acid and conj base are approx equal
Bicarbonate Buffer System
Plays key role in bloods ability to protect against pH changes
CO2 + H2O = H2CO3 = H+ + HCO3-
- H2CO3: carbonic acid is weak acid
- HCO3-: bicarbonate is conj base
Blood pH = 7.35-7.45
- even small deviations from this can cause acidic/alkaline plasma which can be fatal

Solving buffer problems (ICE)
Buffer has 5 mol HCO3- and 5 mol H2CO3 in 10 L H2O
What happens to bicarbonate buffer if 1 mol HCl is added?
- H2CO3 Ka = 4.3 x 10-7
HCO3- + H+ = H2CO3 (don’t inclue Cl-, not acidic)
HCO3- H+ = H2CO3
Initial 5mol 1mol 5mol
Change. -1mol -1mol +1mol
Equilibrium 4mol 0 mol 6 mol
pH = -log(4.3x10-7) + log (4/6) = 6.2 (pH went down as expected)
Estimating log function
log N = x —> N = 10x
log101 = 0 —> 1 = 10x
log1010 = 1
log 10-2 = -2
Hidden Buffer Question
HBr + NH3 –> NH4+ + Br-
1 mol 2 mol 1 mol 1 mol
Not acid and conj base but still a buffer, neutralize each other in 1:1 ratio
Neutralization
Equation
When an acid is neutralized, all of the protons from the original acid have reacted with hyroxide ions from added base
- ratio of acid to base is 1:1 in moles
- Monoprotic acid contains only one acidic proton
- Monoprotic base can only accept one proton
MaVa = MbVb —> for monoprotic acids
- Molarity and volume of acid and base
For diprotic and triprotic acids, have to use normality
Normality can be used for…
Equation
Redox rxns, Precipitations, acid-based chemistry neutralization
N = (mol of OH- or H+ ions) / L solution
- used for polyprotic acids
- for H2SO4, N= 2 mol H+/ 1L
*** at neutralization, normality of acid x volume of acid = N of base x V of base
NaVa = NbVb
Titration definition
2 types of titrations
Technique used to find the concentration of a solution of unknown molarity
- solution is placed in a flask and a diff soln of known conc is added drop-wise
- volume of known soln added is used to determine molarity of unknown soln
analyte: soln of unknown conc
titrate: soln of known conc
2 types of titrations: acid base and oxidation reduction
Acid-Base Titrations
Indicator
Colorimetric titrations: analyte changes color at equivalence point, point when acid or base has been fully neutralized
- use normality eqn: NanalyteVanalyte = NtitrantVtitrant
- eqn only valid at equivalence pt
Indicator: undergo pH-dependent color changes
- occurs once soln pH > pKa of indicator
- indicator pKa should be close to predicted pH at equivalence point
Titration Curves
x-axis is volume base added, y-axis is pH
-
Equivalence point is at pH = 7, complete neutraliation
- at this point **, mole equivalents of acid = mole equivalents of base
-
Half equivalence point is where half of volume of titrant needed to reach equivalence point has been added
- pH = pKa
When a base is titrated with an acid, the curve is flipped from high pH to low pH

Strong acid has ____ conj base
Weak acid has ____ conj base
Strong acids have weak conj bases
Weak acids have strong conj bases
Equivalence point of strong acid/strong base titrations have a pH of
Equivalence point of weak acid/strong base
Strong acid titrated with a weak base has pH
Strong acid titrated with strong base equivalence point pH is 7.
Weak acid/strong base equivalence point pH is always above 7
Strong acid titrated with a weak base has a pH below 7

Polyprotic Titrations
1st proton lost most readily, has highest Ka value
- 2nd and 3rd are harder to lose because they are bonded to an anion
3 pKa values and thus 3 half equivalence points/equivalence points for an acid with 3 protons (H3PO4)

Basic and acidic amino acids
Aminos denature at extreme pH values, have optimal values (7.4 in humans)
For proteins, affects tertiary structure
-
amine group is basic, carboxylic acid group is acidic
- when peptide bond is formed b/w aminos, amine group is bonded to carboxylic group forming an amide which are neutral
- this is why when talking about amino acids acid base chemistry, usually referring to their side chains
Basic aminos have a nitrogen containing side chain
- can gain proton to nitrogen to become positively charged conj acid
- **can act as an acid now if in a basic soln
Both acidic aminos have a side chain with carboxylic acid
- all basic and acidic aminos side chains can exhibit basic and acidic properties

- If glycine is put in an acidic solution, what will happen?
- If put in soln with high pH?
- At neutral pH (normal body conditions)
- Protons attach to amino group (NH3+) and carboxylic acid group (COOH); net charge of +1
- In a soln with high pH, amine group is NH2 and carboxylic acid group is COO-
* net charge of -1 - At neutral pH, NH3+ and COO- –> neutral which is a zwitterion
* all aminos have zwitterion forms, but not all exist as them at physiological conditions
Zwitterion
Electrically neutral ion with both positive and negative charges
multiple pKa’s of amino acids and other compounds
pKa: how acidic a functional group is (likeliness of giving up H+’s)
- lower the pKa, stronger the acid
-
**polyprotic acids have multiple pKa values for each proton they can give up
- **most amino acids will have 3, except for ones without acidic/basic side chains like alanine will have 2 (for amine group and carboxylic acid group)
Lowest pKa is 1
How are pH and pKa of a functional group related?
When pH is equal to the pKa of a functional group, it will be protnated on exactly half of the molecules in solution
- from henderson hasselbalch equation
- carboxyl pKa: 2
- amine pKa: 9
Nonpolar Amino Acid titrations
What type of titration is it?
What is the isoelectric point?
Amino charge at different pH’s?
Each amino acid produces a unique titration curve
Weak acid, strong base titration
- at low ph, functional groups of amino acid all protonated
- at horizontal regions of graph, amino acid soln acts as buffer
***non polar aminos have two pKa values
At half equivalence point 1 (pH 2), half of carboxyl groups deprotonated
- at equivalence pt 1, all of carboxyl groups deprotonated = zwitterions
-
**Isoelectric point(pI): pH at which amino acids net charge is 0
- entire peptides and proteins have pI’s
-
**Isoelectric point(pI): pH at which amino acids net charge is 0
- Half equivalence point 2 is pH 9, half of amine groups deprotonated
- Equivalence point 2 has all of amine groups deprotonated, amino charge of -1
At equivalence point, 1 mol base:1 mol amino, can use to find concentration

Acidic, Basic, Polar amino acid titrations
*3 pKa values instead of 2 for nonpolar aminos
- 3 half equivalence points, 3 equivalence points
- pKa1 =2 (COOH), pKa2 = 4 (COOH of side chain), pKa3 = 9 (NH3)
- pH below 2 has all 3 groups protonated, charge: +1
For acidic aminos(negative): below pH 2, charge is +1; pH between 2 and 4, charge of 0; b/w 4-9 is -1, and pH above 9 is -2
At 1st equivalence point, moles of base added=moles of acid
- this is also the isoelectric point, where molecule is neutral
- for acidic aminos, between two lowest pkas
- for basic aminos, between two highest pkas
Basic aminos titrated with strong acid; start with +2 charge and end at -1
**MCAT treats polar uncharged aminos as having 2 pKa’s, even with side chain
Anatomy of central nervous system
Central nervous system(CNS)- processing sensory info and initiating muscle movement
- brain and spinal cord, both are bathed in cerebral spinal fluid (CSF)
-
both encased in tough membranes called meninges and protected by skull/vertebrae
- meninges consists of 3 layers: dura mater, arachnoid mater, and pia mater
-
both encased in tough membranes called meninges and protected by skull/vertebrae
Peripheral NS
Dictates all other nerves and nervous tissue, including:
- afferent fibers (periphal neurons) that carry info into CNS
-
efferent fibers: carry signals from CNS to periphery
- SAME: sensory afferent, motor efferent
- ganglia: clusters of cell bodies found along sides of spinal cord, in the digestive system, and elsewhere
Brain Divisions
During fetal development, the neural tube forms 3 main regions that give rise to the brain: from anterier to posterior (front to back)
-
Prosencephalon - Forebrain
-
behavior and personality, develops into diencephalon and telencephalon
-
Diencephalon contains:
- thalamus: relays sensory and motor info, regulates sleep
- hypothalamus: regulates homeostasis, communicates between endocrine and nervous systems
- Pineal gland and posterior pituitary gland: secrete hormones
-
Telencephalon:
-
cerebrum: largest structure
- divided into thin outer layer: cerebral cortex (5 lobes)
- hippocampus
- basal ganglia
-
cerebrum: largest structure
-
Diencephalon contains:
-
behavior and personality, develops into diencephalon and telencephalon
- Mesencephalon - Midbrain
-
Rhombencephalon - Hindbrain- more basic functions that have been highly conserved across species through evolution
- Cerebellum‘little cerebrum’: coordination of motor control
-
medulla oblongata: controlls autonomic functions
- breathing and heart rate
-
Pons: a relay station for signals b/w cerebellum, medulla, and rest of brain
- also contains neuron clusters that deal with sleep, respiration, swallowing, taste, bladder control and balance
Limbic system structures
Emotion, motivation, memory
- Cingulate gyrus
- Hippocampus
- Amygdala
- Thalamus
- Hypothalamus
Cerebral cortex lobes (5 but only need to know 4)
1. Frontal lobe: higher level cognition, executive functions
2. Parietal lobe: sensory processing
3. Temporal lobe: sound and language processing, memory consolidation
4. Occipital lobe: primary visual cortex
Responsible for sensation, perception, memory, cognition

Forebrain
Advanced higher-level functions
- behavior and personality, develops into diencephalon and telencephalon
-
Diencephalon contains:
- thalamus: relays sensory and motor info, regulates sleep
- hypothalamus: regulates homeostasis, communicates between endocrine and nervous systems
- Pineal gland and posterior pituitary gland: secrete hormones
-
Telencephalon:
-
cerebrum: largest structure
- divided into thin outer layer: cerebral cortex (5 lobes)
- hippocampus
- basal ganglia
-
cerebrum: largest structure
-
Diencephalon contains:
Hindbrain
Hindbrain- more basic functions that have been highly conserved across species through evolution
- Cerebellum‘little cerebrum’: coordination of motor control
- medulla oblongata: controlls autonomic functions
- breathing and heart rate
-
Pons: a relay station for signals b/w cerebellum, medulla, and rest of brain
- also contains neuron clusters that deal with sleep, respiration, swallowing, taste, bladder control and balance
Midbrain
Motor control, sleeping, homeostatic regulation
- superior colliculus- visual reflexes
- inferior colliculus- auditory reflexes
-
substantia nigra- facilitates coordination of voluntary motor control
- affected by parkinson’s disease
Parkinson’s disease
Progressive neurodegenerative condition characterized by the loss of dopaminergic neurons in the substantia nigra
Brain stem consists of
Midbrain, medulla oblongata, pons
Connects brain to spinal cord
Spinal cord
Contains bundles of sensory/afferent neurons that relay sensory info to the brain and motor/efferent neurons that relay info from brain to muscles
- protected by vertebrae
Conflict theory
Conflict theory states that tensions and conflicts arise when resources, status, and power are unevenly distributed between groups in society and that these conflicts become the engine for social change.
Divisions of Nervous System
Central NS and Peripheral NS
- Central is brain and spinal cord
Peripheral NS is autonomic and somatic NS
- autonomic is divided into sympathetic and parasympathetic
- also enteric: digestion
Peripheral NS
Divided into somatic and autonomic, as well as enteric
- somatic nerves: execute voluntary movement innervating skeletal muscles throughout the body
-
autonomic NS: controls involuntary responses such as sweating and pupil dilation
-
sympathetic: induces fight or flight response under acute stress
- accelerate heart and respiration rates to improve oxygenation of skeletal muscle tissue
- reduce blood flow to organ systems less essential (digestive tract)
- dilates pupils allowing more light to enter, heightening visual acuity
-
parasympathetic: dampens the acute stress response for relaxation and normal physiological functions like digestion
- deescalates body from heightened sympathetic state
- lowering heart rate, constricting pupils
- rest and digest
- deescalates body from heightened sympathetic state
-
sympathetic: induces fight or flight response under acute stress
mobilization of autonomic sympathetic nervous system responses
By epinephrine (adrenaline) and norepinephrine produced by adrenal medulla and some sympathetic neurons

Ganglia are
Sympathetic neuron intermediates that signal to target organs
preganglionic and postganglionic neurons
Which use acetylcholine neurotransmitter?
Ganglia are synaptic relay statins between neurons
Preganglionic neuron synapses at a peripheral ganglion on the postganglionic neuron which then synapses and acts on target organ
- in parasympathetic NS, preganglionic neurons are long; synapse on ganglia near or on target organs
- both pre and postganglionic neurons use neurotransmitter acetylcholine
- in sympathetic system, preganglionic neurons much shorter and synapse on sympathetic trunk- chain of ganglia near spinal cord extending from base of skull to coccyx
- use acetylcholine
- Sympathetic postganglionic neurons are longer and extend to target organ
- don’t use acetylcholine, instead use norepinephrine

Enteric nervous system (peripheral)
Highly complex and semi-autonomous, regulates digestive function
- so complex can be referred to as body’s “second brain”
Nervous system function summary
- Environmental stimuli detected by sensory receptors in bodys periphery
- Transduced into electrochemical signals and transmitted via afferent fibers (SAME)
* carry info to central NS - Info is processed and translated into sensory perceptions by cerebrum
Where 5 senses are processed
Distinct regions of cerebrum for 5 senses
Touch (somatosensation): goes through thalamus, processed in parietal lobe at primary sensory cortex, located on postcentral gyrus (posterior to fold on the brain = central sulcus)
Sight: Signals begin in thalamus and superior colliculus before being processed in occipital lobe before going to primary visual cortex
Sound: first modulated at inferior colliculus before going to thalamus and then primary auditory cortex in temporal lobe
Taste (gustatory pathway): passes through thalamus before ending in gustatory cortex
Motor control pathway (important structures in brain, follow signal)
Signals are modulated by ____ before going down spinal cord
What stimulates muscle contraction?
Coordination is heavily dependent on…
Initiated in premotor cortex, executed by primary motor cortex located on the frontal lobe at structure called precentral gyrus (anterior to postcentral gyrus) bordering central sulcus (fold)
- Electrochemical signals generated in primary motor cortex are modulated by:
- cerebellum and basal ganglia, substantia nigra
- coordinates contraction of different muscle groups to unify movement
- then proceeds down spinal cord to efferent neurons which terminate at a neuromuscular junction
- releases acetylcholine on muscle cell, stimulating contraction
- cerebellum and basal ganglia, substantia nigra
**Coordination is heavily dependent on dopamine, the prominent nerve transmitter in the brain
- dopamine disregulation implicated in Parkinson’s
Efferent fibers synapse acetylcholine on…
Muscle cells, including smooth and cardiac muscle of internal organs
Important neurotransmitters
Acetylcholine- muscle contraction
Norepinephrine-
Dopamine-
Glutamate- amino acid, primary excitatory nerve transmitter
- responsible for neuron depolarization and elicitation of action potentials
GABA: most prominent inhibitory neurotransmitter
- hyperpolarizes neurons, reducing likelihood of firing
Neuron structure
Rapid relay of signal; non-dividing highly specialized and electrically excitable cell
- require a lot of support and maintanence - Glial cells
- neurons very demanding metabollically, require constant glucose influx by astrocytes (subtype of glial cells)
- Signal input - dendrites
- Signal output- terminal
Soma- cell body; contains nucleus and all cellular organelles
- Between soma and terminal is the axon, which relays signals
Dendrites face a synaptic cleft (small gap b/w two neurons) between them and terminal end

Blood-brain barrier
astrocytes: Glial cell which transforms nutrients for neurons with help of epithelial cells and pericytes (surround/support epithelial cells)
- form blood-brain barrier: links neurons and CNS to blood supply
Blood brain barrier is selectively permeable to specific substances, helps maintain stable environment for neurons
Glial cells and subtypes
Glial cells provide nutrients, structure, insulation, and defense from pathogens - many subtypes with specialized functions:
-
astrocytes: transform nutrients with epithelial cells and pericytes (surround/support epithelial cells)
- form blood-brain barrier: links neurons and CNS to blood supply
- ***astrocytes also function as constant, insulin independent active transport of glucose from blood stream to neurons
- satellite cells: nutrient support and protection
- ependymal cells: secretes cerebral spinal fluid
Insulation of neurons (myelination)
What provides myelin?
Function of myelination
Insulation provided by oligodendrocytes in CNS and Schwann cells in peripheral NS
- wraps axon in a sheet of a white, fatty substance called myelin
- leaves small gaps called nodes of Ranvier
Not all nerves myelinated, but serves purpose of preventing cross-talking b/w axons and speeds of signal transmission
- action potential travels from one unmyelinated gap to the next–> jumping down axon (saltatory conduction)

Microglia
First line of defense for central NS
- function like macrophages
- also remove waste in damaged cells, prune some neurons, and eat away extracellular protein deposits
Cerebrospinal fluid
Bathes/buffers cells of central nervouse system
- fluid is secreted and circulated by ependymal cells (type of glial cells)
Constant stable chemical environment and physically cushions the CNS
Signal Transmission (neurons)
Terminal end of one neuron releases neurotransmitters across synaptic cleft which bind to receptors on dendrites of another neuron allowing influx of specific ions
- causes a change in membrane potential = graded potential; the more neurotransmitters that bind, the more graded potentials created
- graded potentials can travel along the dendrites and soma to the axon hillock, next to axon
- axon hillock is next to voltage-gated sodium channels
- graded potentials can travel along the dendrites and soma to the axon hillock, next to axon
If enough graded potentials add up to reach threshold potential (-55mV), action potential is generated and travels down axon
- once action potential reaches terminal, causes calcium channels to open up; influx of calcium creates signaling cascade which leads to exocytosis of neurotransmitters
Membrane Potential
Membrane of cells is nonpolar and impervious to ions with exceptions like Na+/K+ ATPase transporter
- ability to regulate entry/exit of specific ions creates membrane potential
- difference in electric potential on each side of membrane; **difference in distribution of charged particles b/w two locations
- measured in volts
- difference in electric potential on each side of membrane; **difference in distribution of charged particles b/w two locations
More positively charged cells on outside than inside = negative membrane potential
- know this:**inside of cell is rich in negative aminos and K+, outside of cell is rich in Ca2+, Na+, and Cl-
- overall negative membrane potential of -70 mV
Na+K+ ATPase
Enzyme that hydrolyzed ATP to push 3 Na+ ions out of cell for 2 K+ ions
- constitutively expressed in all cells and is always active, accounts for much of cells hydrolyzed ATP
- gives cell resting membrane potential of -70 mV
Depolarization of membrane potential
Overshoot of membrane potential
Repolarization
Hyperpolarization
Depolarization: membrane potential becomes less negative and approaches zero
Overshoot: membrane potential becomes positive
Repolarization: returning to the resting membrane potential after the neuron has depolarized (-70 mV)
Hyperpolarization: membrane potential becomes more negative than resting membrane potential -70 mV
Voltage gated channel
Usually for Na+
Opens/closes in response to change in membrane potential

Graded potentials (different types)
Dendrites contain specific receptors for different neurotransmitters; when a neurotransmitter binds, it allows an ion to flow inside which changes the membrane potential of the cell = graded potential
- most graded potentials are excitatory:
- Excitatory Postsynaptic Potentials (EPSPs): raise membrane potential, making it more positive
- Inhibitory Postsynaptic Potentials (IPSPs): make membrane more negative =hyperpolarization
Spatial and temporal summation: potentials add up if located close to each other or happen in short time span
What happens when threshold potential of a neuron is reached?
Once graded channels add up to threshold potential (-55 mV), voltaged gated sodium channels open up and, like a flood, sodium rushes into cell down its concentration gradient and electrical gradient
- causes membrane potential to increase even further opening up neighboring sodium channels
- **this causes chain reaction, as there are sodium channels all along the axon
Action potential: cascade of depolarization down the axon
Repolarization of neuron after action potential fires
Voltage gated potassium channels open up, closing voltage gated sodium channels at abot +35 mV
- loss of cations quickly makes membrane potential negative again, overshooting and causing hyperpolarization
Potassium channels close and **Na+ K+ ATPase brings membrane potential and concentration gradient back to resting
Refractory period of neurons (2 types)
Once voltage gated sodium channels close at depolarization peak (~ +40 mV), cannot open again for a certain period of time: absolute refractory period
- new action potential won’t initiate
- serves as a safety check, prevents signal from traveling backwards
Relative refractory period: Na+ channels are able to open again, but the membrane is still hyperpolarized; possible but difficult to generate action potential
What happens when action potential reaches terminal end of neuron?
Instead of sodium channels, terminal end of axon has voltage gated calcium channels
- open in response to depolarization/action potential
- opening creates an influx of calcium which causes chemical signaling cascade resulting in exocytosis of neurotransmitters from vesicles into synaptic cleft of next neuron
- vesicles: dedicated storage structures that fuse w/ plasma membrane of terminal
- opening creates an influx of calcium which causes chemical signaling cascade resulting in exocytosis of neurotransmitters from vesicles into synaptic cleft of next neuron
What happens to neuroteransmitters after binding to neuron receptor?
Either undergo degradation or reuptake
-
degradation: hydrolytic enzymes break neurotransmitter apart
- ex. acteylcholinesterase: catalyzes breakdown of ester linkage of acetylcholine
- strong/immediate effects
- ex. acteylcholinesterase: catalyzes breakdown of ester linkage of acetylcholine
-
reuptake: neurotransmitters moved out of synaptic cleft by presynaptic neurons or by astrocytes
- __various transport proteins in membrane of presynaptic neuron
- for monoamines (norepinephrine, dopamine, serotonin), reuptake is followed by breakdown by monomine oxidases
Regulation of neurotransmission by exogenous chemicals (from outside the body)
Selective Serotonin Reuptake Inhibitors (SSRIs): treatment of depression
Monoamine Oxidase Inhibitors (MAOIs): anti-tuberculosis, anti-depressant
Electrical neuron synapse
Sending and receiving neurons are closer together, linked by gap junctions
- allows for direct diffusion of neurons, membrane potential of one neuron can immediately influence that of the other
- * speeds up signal transmission but can’t amplify/modulate the signals
How do sensory neurons get triggered?
3 types of receptors
External stimuli has to trigger a graded potential;
- Thermoreceptor: heat
2. Baroreceptor: pressure
3. Photoreceptor: light
Membrane capacitance
Capacitance: how much charge is on both sides of an insulator and thickness of insulator
- insulator is cell membrane
- Charging/discharging membrane requires work, higher the membrane capacitance the more difficult it is to change membrane portential
- neuron harder to depolarize (larger neurons)
Larger neurons have more area to store charge along membrane and therefore have higher membrane capacitance = harder to depolarize
Membrane resistance and Cytoplasmic resistance in neurons
Membrane resistance: ability of membrane to keep charges separate
- high membrane resistance = effective action potential transmission
- low membrane resistance can cause leakage of ions
Cytoplasmic resistance: how much the cytoplasm itself impedes the flow of ions
- higher the cytoplasmic resistance, slower the neuron conduction
- **larger the neuron, lower the cytoplasmic resistance
Small vs. large neurons
Capacitance: the ability of a system to store an electric charge.

How signals travel at fast speeds across long neurons
Membrane resistance, membrane capacitance, and cytosolic resistance will determine conduction speed
myelination: drastically decreases membrane capacitance and increases membrane resistance
- wrapping axon in thick lipid layer; insulating large portions of the axon
- prevents efflux (outflow) of ions (by increasing membrane resistance)
Decreases capacitance: thick layer between cytoplasm and extracellular fluid
**Depolarization decays along these portions, which is why unmyelinated Nodes of Ranvier are necessary to replenish it
Nodes of Ranvier
Intermittent, short unmyelinated regions of axon; all usual players are highly abundant (sodium/potassium channels, Na+K+ ATPase)
- depolarization decays slightly in myelinated regions
- when going through Nodes of Ranvier, voltage gated sodium channels open and depolarization is replenished to full intensity
Failing to maintain myelination of axons
Hallmark of debilitating neurological diseases
- multiple sclerosis
Nernst equation
Retina
Cones and Rods
Eye: detect visual stimuli (light) –> action potentials –> brain
Retina: turns certain wavelengths of light into action potentials, located at the back of the eye
- contains millions of photoreceptors (cones and rods)
-
cones responsible for perceiving color and fine detail
- 3 diff types for different wavelengths: short, medium, long wavelength
- short: perceives blue, 420 nm
- medium: perceives green, 530 nm
- long: perceives red, 560 nm
- 3 diff types for different wavelengths: short, medium, long wavelength
-
cones responsible for perceiving color and fine detail
Cones are centralized in the fovea centralis of the retina, a small pit that only contains cones
- also in the macula, central region around the fovea
Rods don’t sense color: sensitive to visual input, don’t pick up on detail well, responsible for night vision; black and white
- contain rhodopsin compound, pigment that doubles as photoreceptor proteins - sensitive to light
Many more rods than cones, distributed away from center of retina - peripheral vision best for seeing dimly-lit objects at night
C for cones = color
R for rods = rhodopsin, black and white

Lens and cornea
Cilliary muscle and cilliary body
Anterior and posterior chamber
Eye converges light on retina to display a clear image
Lens and cornea located at the front of the eye
-
cornea: very first thing light passes through to enter the eye
- used for protection and focusing light
-
lens: finishes focusing light
- can change shape to help eye focus on objects at diff distances
Cilliary muscle apart of larger cilliary body, used to adjust lens via suspensory ligaments
-
Anterior chamber- smaller, front facing area
- contains aqueous humor fluid
-
Posterior chamber- larger space towards back of eye
- contains vitreous humor fluid

Iris, pupil
iris: colored part of eye with hole in its center = pupil
- pupil lets light into eye, iris is sun shield
Iris is connected to two muscles to help deal with varying levels of light
- dilator pupillae: increases pupil size (pulls iris back); allows more light (happens in the dark)
- constrictor pupillae: decreases pupil size (extending iris), allows less light
Sympathetic NS kicks in –> fight or flight –> pupils dilate
Parasympathetic NS –> rest and digest –> constrict
Choroid and sclera
Choroid= middle layer, vascular tissue that supplies retina with blood and absorbs excess light
- forms a continuous layer with the iris
Sclera= outermost layer, continuous with the cornea and accounts for white color of eye
Steps between light ray hitting retina and action potential being sent through optic nerve to brain
Bipolar cells, ganglion cells, horizontal cells
- Cones and rods don’t directly connect to optic nerve; instead, synapse onto neurons known as bipolar cells- called bipolar due to shape
- bipolar cells accept info from multiple cones/rods
- Horizontal cells: in between photoreceptors and bipolar cells; inhibit photoreceptors helping eye to edjust to high light
- Bipolar cells synapse with ganglion cells, components of the optic nerve
* mediated by amacrine cells

Visual fields and optic nerve
Two visual fields, one for seeing the left and right sides
Each retina field is also divided into two halves, with the left side of the retina corresponding to the right side of the field and vice versa
- ** a light ray to your left will bounce off the right side of retina in both eyes
Optic nerve has four components, one for each half of each retina
- Two optic nerve components cross at optic chiasm (innermost halves of both eyes) = nasal halves (closest to the nose)
- cross over and lead to opposite sides of brain
Input on the outermost halves stay on the same side of brain
**input from the left facing halves of both eyes (right visual field) gets processed on the left hemisphere of brain, input on right facing halves (left visual field) gets processed on the right

Optic tract, temporal and spatial resolution
Optic tract: bundles of nerves carrying visual info to each brain hemisphere from the optic nerve
Optic tract runs through the lateral geniculate nucleus, structure in the thalamus that is main relay station for input from retinas
- contain specialized neurons
-
magnocellular neurons: large neurons, specialize in detecting motion
- m for motion
- Temporal resolution: ability to pick up changes
-
parvocellular neurons: small, good at picking up details but not motion
- spatial resolution: ability to see in detail
-
magnocellular neurons: large neurons, specialize in detecting motion
Visual input further processed in occipital lobe
Motion Parallax
feature detection and parallel processing
serial memory processing
Objects that are close to us move further across our visual field than objects that are far from us
- cues for perceiving depth
feature detection: detection of individual stimuli
parallel processing: integrating multiple inputs simultaneously
serial memory processing: systematically giving attention to one thing at a time
- looking for your keys
MCAT most often tests vision and hearing in detail
Sound
Sound waves are longitudinal waves that, in air, manifest as regularly repeating changes in pressure as air molecules move back and forth
Ear is a funnel that gathers these waves and converts them to neural signals
Vestibular sense
Hair cells in inner ear (organ of Corti) help with balance and our orientation in 3D space - swaying motion in endolymph turned to neural signals
- within inner ear, 3 endolymph containing structures called semicircular canals responsible for sensing rotational acceleration
- when the head rotates, endolymph moves and hair cells resist that motion
- sends signal to the brain
Semicicular canals arranged perpindicularly like XYZ axes
Inner ear also contains vestibule, which senses linear acceleration
- contains utricle: detects horizontal motion
- saccule: detects vertical motion

How do we hear?
Cells responsible for converting sound waves to neural signals are hair cells because they have stereocilia (look like hairs) that poke out into fluid called endolymph
- Sound waves cause stereocilia to move in endolymph which opens up ion channels of the hair cells
- allows small positive ions into cell
- triggers an influx of calcium ions through voltage gated calcium channels which releases neurotransmitters at the other end of the cell

Organ of corti
Ear is divided into outer, middle, and inner ear
- hair cells (which pick up sound waves) are located in the inner ear in a structure called organ of Corti = layer cake
- organ of corti consists of basilar membrane on bottom, hair cells in endolympth in the middle, and tectorial membrane above
Sound waves enter ear and cause hair cells to vibrate in endolymph, release neurotransmitters that trigger nerve signals to the brain
Outer Ear
Auricle: cartilaginous external ear above the ear lobe
- funnel incoming sound waves into auditory canal which leads to ear drum
-
ear drum (tympanic membrane): vibrates in response to sound waves
- high frequency waves = high freq vibrations
*
- high frequency waves = high freq vibrations
-
ear drum (tympanic membrane): vibrates in response to sound waves
Middle ear
Contains ossicles: 3 tiny bones that fit together to amplify the vibrations (by as much as 10x) of the tympanic membrane (ear drum)
- malleus connected to ear drum
- sends vibrations to the incus
- incus connects to the stapes
Stapes connects to the oval window, boundary between middle ear and inner ear - sends amplified vibrations to inner ear
Middle ear also contains a connection to the nasal cavity: Eustachian tube: valve that equalizes the pressure between middle ear and environment (ears popping)
Inner ear
Bony labyrinth: basic framework of inner ear
Area between bony labyrinth and membranous labyrinth contains perilymph, fluid similar to endolymph
-
membranous labyrinth: within bony labyrinth, makes up sub-structures of inner ear
- contains endolymph
Cochlea: Structure responsible for hearing; spiral shaped and divided into three layers called scalae
- middle layer contains organ of corti
-
hair cells protrude from basilar membrane, bathed in endolymph
- layer below is filled with perilymph, vibrates in response to sound which are transferred to basilar membrane
-
hair cells protrude from basilar membrane, bathed in endolymph

Basilar membrane
How aging affects hearing?
Receives vibrations from organ of Corti
-
Place theory: thickness of basilar membrane isn’t constant
- different thicknesses respond to different frequencies
- thickest in response to high frequency vibrations at its base, next to oval window
- narrowest at apex
- Allows brain to infer the pitch of a sound based on which hair cells send signals
As we age, damage to hair cells and stiffening of basilar membrane contribute to age-related hearing loss

Ear divisions
Outer ear: gathers sound waves
Middle ear: amplifies
Inner ear: sound detection, organ of Corti
auditory processing from organ of Corti
Left hemisphere is used for?
Right hemisphere?
Nerve signals generated by hair cells are transmitted through vestibulocochlear (auditory) nerve
- passed through medial geniculate nucleus in the thalamus on the way to auditory cortex in the temporal lobe
Left hemisphere- speech
Right hemisphere- background noise, music
Touch
two point threshold
physiological zero
Somatosensation: touch, pain, temperature, pressure, stretching
Nerves in body aren’t distributed evenly, some areas are more dense
- tips of fingers more sensitive, skin on back of head insensitive
two point threshold: minimum distance for distinguishing two point stimuli
- the denser the nerve distribution, the smaller the two point threshold
Physiological Zero: reference point of our skin, call temp hot or cold based on this
- skin is usually cooler than core body temp

Gate theory of pain
Body can turn pain signals on or off in the spinal cord
- Intensely painful stimulus can override less painful one
- different people have different pain thresholds
Differences between taste and smell receptors
Both taste and smell use chemoreceptors
-
Olfactory (smell) receptors respond to huge range of stimuli dissolved in the air
- processed in olfactory bulb then passed to olfactory tract
- then processed by other parts including limbic system (emotion)
- processed in olfactory bulb then passed to olfactory tract
-
Gustatory (taste) receptors pick up smaller range of tastes of substances dissolved in fluids
- processed in thalamus then sent to gustatory cortex
Sensation vs. Perception
Sensation doesn’t equal perception
sensation: real, physical objects information is detected by our body (objective)
perception: our brains personal experience of sensory information (subjective)
Sensory receptors - communicate four properties to central NS
Specialized dendrites of sensory neurons that respond to various physical stimuli - action potentials sent to CNS
- bundled together into ganglia (cluster of nerve cells)
4 properties communicated to CNS:
- location: where stimulus is coming from
- modality: type of stimulus
- intensity: how strong the stimulus is
- duration: how long a stimulus lasts
Types of sensory receptors
Exteroreceptors: respond to stimuli from outside world
- 5 senses
Interoreceptors: respond to internal stimuli
- can sense internal pain
- dehydration/overhydration
-
baroreceptors: detect pressure inside the body, like walls of blood vessels
- blood pressure linked to blood volume and hydration
-
osmoreceptors: detect concentration of solutes in blood
- triggers responses when blood becomes too dilute or concentrations
-
propioreceptors: found in and around muscles, tendons, joints
- responsible for giving kinesthetic sense of relative position of the parts of our body in space
-
baroreceptors: detect pressure inside the body, like walls of blood vessels
Receptors responsible for taste and smell?
Olfactory receptors: sense of smell
- respond to volatile chemicals (chemicals in air)
- sensitive to near limitless range of chemicals
Gustatory receptors: sense of taste
- respond to chemicals dissolved in saliva
- more limited
Both response to chemical stimuli

Receptors responsible for vision and hearing?
Photoreceptors: responsible for vision reception
- respond to specific wavelengths of light
Hair cells: responsible for sound reception
- convert pressure signals from sound waves into action potentials
- also use pressure to respond to rotational acceleration (balance)
- semicircular canals
- hair cells in crista ampullaris send rotational info to NS
Receptors responsible for touch
Mechanoreceptors: respond to mechanical stimuli
- different types detect different stimuli (don’t need to memorize)
- tactile corpuscles: detect light touch
- merkel nerve endings: respond to sustained pressure
- Ruffini endings: sense deep pressure beneath surface of skin
- Pacinian corpsucles: detect high frequency vibrations
Receptors that detect pain
Nocireceptors detect pain, mechanical, chemical and thermal stimuli
Proximal and distal stimuli
Proximal stimulus: what the sensory receptor picks up on
Distal stimulus: environmental source of signals
Absolute threshold
Threshold of conscious preception
Absolute threshold: Level of intensity that a stimulus must have in order to be picked up by sensory neurons
- if a stimulus doesn’t hit threshold, not registered by our bodies
- experimental design minimizes any other influences
Threshold of conscious preception: threshold a stimulus must cross in order for our bodies to consciously perceive it
- other factors can distract even if stimuli crosses absolute threshold

Just Noticeable Difference (of stimuli)
Weber’s Law
**know this
Smallest change in magnitude of a stimulus that we can perceive as being different
- psychophysical discrimination testing
Weber’s Law: for any given sensory input, the just-noticeable difference will be a constant proportion of the original output
- ex. can detect 10% increase in weight = 1 to 1.1 lbs, 10 to 11 lbs; 100 to 110 lbs
- can’t detect 100 to 105
- Breaks down at extremes (too strong, too faint)
Signal Detection theory
Want to maximize hits and correct rejections, minimize misses and false alarms
Signal detection can vary across people and psychological states
Relevant to diagnosing medical conditions

Sensory Adaptation
Getting used to stimuli, blocking out other stimuli
- partly occurs in brain, primarily in sensory receptors
Tonic receptors: receptors that are slow to adapt to stimuli
- respond as long as the stimuli is present
- stretching, pain
Phasic receptors: send a burst of action potentials, then stop (fast adaptation)
- hair follicles
Two types of processing for perception
Bottom up processing: brain starts with individual pieces of sensory info and assembles them into a coherent whole
Top down processing: brain decides what its looking for ahead of of time and assembles individual pieces in a way that supports the picture
Both types coexist for all of our senses
- hearing a song then trying to recognize what the name is
Gestalt Principles of Grouping (principle of proximity, similarity, and good continuation, closure, symmetry)
Law of Pragnaz
Principle of proximity: we perceive objects or shapes close together as forming groups
Principle of similarity: objects similar in some way will be perceived in a group
Principle of good continuation: if multiple objects overlap, perceived as a continuation of few objects
** principles don’t apply in isolation
Principle of closure: We infer the presence of complete shapes even when they’re incomplete
Principle of symmetry: symmetrical objects more likely to be perceived as parts of a whole than asymmetric
Law of Pragnaz- overall, objects perceived in the simplest most meaningful ways
Depth
- Depth- ability to perceive a third spatial dimension
- near vs. far in addition to up/down, left/right
- perceived using binocular eye clues (both eyes)
Endocrine system vs exocrine glands?
Merocrine?
Apocrine?
Holocrine?
-crine = secrete
Endocrine system is a collection of organs and tissues whose job is to produce/release hormones at the right times DIRECTLY into circulation
-
exocrine glands: secrete their products through a duct
- ex. salivary glands, liver and pancreas, sebaceous glands (secrete skin oils)
- ACT LOCALLY, can’t affect organs or tissues at a distance
Merocrine: release products through exocytosis
- sweat glands
Apocrine: releases products by membrane budding
Holocrine: release products via membrane rupture and cell lyse
Endocrine glands release…
Most important endocrine glands
Endocrine glands release hormones (signaling molecules) into bloodstream to act on target tissues from a distance
- certain hormones can also function as neurotransmitters dpending on HOW its secreted
- norepinephrine, oxytocin, antidiuretic hormone
Hypothalamus, pituitary gland, thyroid, adrenal gland, pancreas

Organs with endocrine and exocrine function
Pancreas:
- has pancreatic islets with endocrine functions
- releases key hormones like insulin and glucagon
-
acinar cells with exocrine functions
- release digestive enzymes into GI tract through pancreatic duct
Tropic vs. Non tropic hormones
Tropic hormones: target other endocrine glands, usually stimulate release of another endocrine hormone
- most are produced and secreted by hypothalamus and anterior pituitary gland
- give more opportunities for processes to be regulated (more important implications)
Non-tropic (DIRECT) hormones: act on non-endocrine tissues
- cause direct physiological effect
Some common uses for synthetic hormones
Synthetic estrogens and progestrogens, oral contraceptives
Thyroid hormone thyroxine to treat hypothyroidism
Steroid hormones for autoimmune diseases
Injectable insulin for diabetes
ACE inhibitors lower blood pressure by inhibiting angiotensin converting enzyme
3 major classes of hormones
Peptide hormones, steroid hormones, amino acid derivatives
Peptide hormones
vs.
Steroid hormones
Essentially peptides varying in amino acid number/length of aminos
- HYDROPHILIC; diffuse freely into bloodstream, no need for blood transport proteins
- However, CAN’T diffuse through cell membranes, must bind to extracellular receptors
- intracellular second messagers then elecit desired effect
- ex. cAMP, Ca2+, IP3
- intracellular second messagers then elecit desired effect
- However, CAN’T diffuse through cell membranes, must bind to extracellular receptors
- Rapid, short time changes
Steroid hormones are derived from the lipid cholesterol and contain its characteristic 4 ring structure
- HYDROPHOBIC; ride carrier proteins in the blood stream
- carrier protein examples: sex hormone binding globulin, albumin
- easily diffuse through cell membranes and bind with receptors (usually nuclear receptors that function as transcription factors)
- Triggers conformational shift that ACTIVATES receptor –> binds to DNA and promotes/represses transcription
- effects take a while, last longer than peptide homrones
- carrier protein examples: sex hormone binding globulin, albumin
Where are steroid hormones produced?
How are peptide hormones produced
Steroid hormones synthesized from cholesterol in the smooth ER and diffuse directly through cell membrane into bloodstream
Peptide hormones produced by transcription of relevant mRNA, translation into polypeptide –> preprohormone
- preprohormone is secreted into rough ER and modified into prohormone –> golgi apparatus
- in golgi, cleaved by peptidases and sometimes modified by glycosylation into peptide hormones
- leave golgi in vesicles
Amino acid derived hormones
Some behave like peptide hormones, some behave like steroids
Small molecules derived from a SINGLE amino acid
- ex. T3 and T4 hormones derived from tyrosine - both hydrophobic, behave like steroid hormones w/ long lasting effects
Others like epinephrine and norepinephrine are water-soluble and act like peptide hormones - powerful but short lived
Some are amphipathic
How does endocrine system know when to release hormones?
What happens when youre stressed?
Neuroendocrine integration: nervouse system senses changes in environmental conditions and communicates to endocrine system
-
hypothalamus in the brain responds to nervous system input and secretes tropic hormones that stimulate the production of other hormones from the pituitary gland
- __pituitary hormones act on organs throughout the body
- Nervous system notifies hypothalamus which releases the tropic hormone corticotropin-releasing hormone (CRH) which
- binds to anterior pituitary gland which then releases adrenocorticotropic hormone (ACTH)
- ACTH acts on adrenal cortex which secretes cortisol into circulation
Cortisol- steroid hormone released during periods of long term stress
Cortisol
Pathway that leads to cortisol release is called…
Regulation of this pathway by…
Steroid hormone released during periods of long term stress
Increases metabolism of fats, proteins, and sugars
- if chronically elevated, can lead to weight gain, immune suppression, and increased risk of diabetes
Hypothalamic-Pituitary-Adrenal
- Nervous system notifies hypothalamus which releases the tropic hormone corticotropin-releasing hormone (CRH) which
- binds to anterior pituitary gland which then releases adrenocorticotropic hormone (ACTH)
- ACTH acts on adrenal cortex which secretes cortisol into circulation
Cortisol regulates pathway by negative feedback by inhibiting CRH and ACTH
However, hypothalamus and pituitary gland gradually become less sensitive to it if stress continues, cortisol levels can elevate
Almost all feedback pathways in the endocrine system are…
Negative feedback loops - downstream product feeds back to inhibit earlier point in pathway
- prevent physiological parameters like blood pressure and blood glucose from getting too high or low
Positive feedback in the endocrine system
Much less common than negative feedback
- Oxytocin pathway:
- Oxytocin is peptide hormone secreted by the posterior pituitary
- stimulates uterine contractions during labor
- First uterine contractions stimulate the release of more oxytocin
- induces stronger uterine contractions
- Amplifies until baby is born

Gonads vs. Genitalia
Male reproductive external anatomy
Gonads: where gametes are made
- in males, gametes are sperm and gonads are testes
Genitalia: internal and external reproductive organs
- in males, external genitalia are penis and scrotum (ballsack)
Testes: site of spermatogenesis: production and maturation of male gametes
- secrete androgens (sex hormones, testosterone)
- functions best at a few degrees below body temperature
Testicular thermoregulation: position of the scrotum is controlled by two muscles
- the cremaster: contracts to draw testes closer to the body
- and dartos muscles: contracts to wrinkle the scrotal skin
Within the testes ____ takes places
Spermatogenesis takes place in a series of coiled tubes = seminiferous tubules, separated by barriers called septa
- Production of spermatazoa (sperm) from germ cell precursors is facilitated by Sertoli cells, which make up epithelium of seminiferous tubules
Next to seminiferous tubules are endocrine cells called Leydig cells, secrete androgens such as testosterone
- immature spermatazoa goes from tubules to the epididymis **used for storage and maturation of sperm
- nonmotile in epididymis, gain motility over period of 2-3 months
- either ejactulates or gets reabsorbed
- nonmotile in epididymis, gain motility over period of 2-3 months

When ejaculation occurs
Sperm travels from epididymis (storage and maturation) to the vas deferens which connects to ejactulatory ducts, formed by fusion of vas deferens with seminal vesicles
Seminal vesicles: generate majority of semen liquid component; nutrients like fructose, vitamins, enzymes
Ejaculatory ducts travel through prostate gland and then join with the urethra
- Cowper’s gland (bulbourethral): produce preejaculate which lubricates the urethra, neutralizes acidic urine
SEVE UP (picture)

Spermatazoa vs. Semen
What is Azoospermia?
Spermatazoa: haploid gametes that fertilize eggs
Semen: alkaline nutrient filled liquid
- carries sperm through reproductive tract
- **Basic as a buffer from acidic environment of female reproductive tract, protecting DNA from degradation
Azoospermia: semen containing no sperm
Internal female genatalia
External female genatalia
Internal: Ovaries, fallopian tubes, uterus, cervix, vagina
External genatalia collectively known as vulva: labia majora, labia minora, clitoris, vaginal orifice, urethral opening
- labia minora: helps protect urethral opening from irritation/infection
- clitoris: sex organ,
Oogenesis is
Ovaries two functions:
Production of female gametes, occurs in the ovaries (female gonads)
- results in the production of mature ova “eggs”
- contain many follicles, each of which houses immature egg called oocytes
- all PRIMARY oocytes are produced before birth, ~400,000 follicles at start of puberty
Ovaries also have endocrine function, producing estrogen and progesterone
Ovulation and ovum journey
Ovulation: during each menstrual cycle, one follicle releases secondary oocyte into the peritoneal cavity
- ovum is swept up into fallopian tubes by cilia, transported to uterus by cilia and peristaltic contractions of smooth muscle
If an ovum is fertilized by sperm in the fallopian tubes, then implants in the wall of uterus where fetus develops during pregnancy
3 layers of the uterus
1. Endometrium: innermost layer, mucous membrane of epithelial cells that thickens and thins over course of menstrual cycle in anticipation of implantation
2. Myometrium: smooth muscle
3. Perimetrium: outer layer
Cervix and vagina
-
Cervix: Cylindrical structure that connects the uterus to the uterine cavity
- sperm must travel through cervical canal and uterus for fertilization
- connects to vagina
-
Vagina: elastic walls allow vaginal canal to stretch and accomodate a fetus during childbirth
- also home to a rich population of bacteria, maintaining healthy microbiota is important aspect of reproductive health
Spermatogenesis
Male gametogenesis which produces spermatazoa
- Begins with spermatogonial stem cells which can follow one of two paths:
- divide to form more stem cells
- differentiate into spermatogonia
-
Spermatogonia (diploid) undergo spermatogenesis, start by mitosis
- Form two spermatocytes
- Then undergo meiosis I
- __2 haploid, sister chromatids (two copies of each chromosome)
- __Secondary spermatocytes undergo meiosis II to form 4 haploid spermatids with one copy of each chromosome
Spermatids undergo spermiogenesis
- formation of tail
- loss of excess cytoplasm
- formation of acrosomal cap- enzymes required for fertilization
- still not motile - gain this in epididymis
Mature sperm cell has 3 parts:
- Head: cells nucleus, surrounded acrosomal cap
- Midpiece: abundant mitochondria, provide energy
- Tail: provides motility
Steps of oogenesis
-
Oogonia formed by primordial germ cells
* just like in spermatogenesis, differentiate into primary oocytes
2. Undergoes meiosis I, EXCEPT halted in prophase I until puberty
- beginning at puberty, small number of oocytes resume oogenesis
3. Diploid cell divides into one haploid (1n) secondary oocyte and one polar body (receives much less cytoplasm, dies) - secondary oocyte is released from ovarian follicle each month
4. IF FERTILIZED, resumes meiosis II, creating a zygote and a second polar body
Hypothalamus functions
Almond sized region of the forebrain, bridge between nervous and endocrine systems
- controls autonomic activities like body temp, metabolism, fatigue, sleep
Also oversees activity of the pituitary gland, which regulates other endocrine glands
Pituitary gland consists of:
Similarites b/w lobes:
Consists of anterior and posterior glands lobes; both of which receive input from hypothalamus but in different ways
- anterior lobe: receives input via hormonal signals
- posterior lobe: receives input via neuronal signals
Similarities: both secrete peptide horones, both receive hypothalamic input
Anterior pituitary gland and the hypophyseal portal system
Receives hormonal input from hypothalamus
- Physically connected to hypothalamus via hypophyseal portal system: system of blood vessels at the base of the brain
- contains extremely permeable endothelial (blood and heart cells) cells
- **allows for exchange of hormones/other small molecules
- Regulates anterior pituitary hormone production with tropic hormones –> leads to secretion of other tropic hormones
- contains extremely permeable endothelial (blood and heart cells) cells
Tropic hormone naming patterns
Major hypothalamic tropic hormones
Hypothalamic tropic hormones are “something-releasing hormone”, something referring to next tropic hormone in pathway (usually anterior pituitary hormone)
Anterior pituitary hormones named “something-stimulating hormone”, referring to next and final hormone in pathway
ex. thyrotropin releasing hormone (TRH) tells anterior pituitary to release thyroid stimulating hormone (TSH) which tells thyroid to produce T3 and T4
ex. gonadotropin releasing hormone (GnRH) which tells anterior pituitary to release LH and FSH which play roles in reproduction and growth
- in males LH, stimulates Leydig cells in testes to release testosterone and FSH promotes spermatogenesis
- in females, LH stimulates estrogen production from ovaries, FSH promotes maturation of ovarian follicles
ex. corticotropin-releasing hormone (CRH), releases adrenocorticotropic hormone (ACTH) which travels to adrenal cortex and produces corticosteroids: stress response and circadian rhythms

Anterior pituitary hormones (not from hypothalamus activation)
Prolactin: acts on the mammary glands to stimulate milk production
Endorphins: reduce reception of pain
Non tropic endocrine hormones - Thyroid
Thyroid is located on the front of the trachea
- secretes T3 and T4 which increase metabolic rate
- Hypothyroidism: slow metabolic rate - weight gain, fatigue
- Hyperthyroidism: accelerates metabolic rate - weight loss, tachycardia
Thyroid also secretes the hormone calcitonin: reduces calcium concentration in the blood stream
- promotes storage of Ca in bone, increases urinary excretion of calcium
- “toning down” calcium in blood
Posterior pituitary gland
two main posterior hormones
Bundle of neuronal axons whose cell bodies originate in hypothalamus
- extension of hypothalamus
- all of hormones released are synthesized in hypothalamus, travel down neuronal axon and are stored in posterior pituitary until signaled by hypothalamas
2 main hormones:
- Oxytocin: contractions during labor
- Anti-diuretic hormone (ADH): helps maintain fluid balance in body, released when blood volume gets too low and osmolality (salt conc) is too high; also increases blood pressure
- blocks diuresis (urine production) to help body maintain fluid
- promotes water reabsorption in kidneys
Parathyroid Glands
Release parathyroid hormone: opposes effects of calcitonin in order to increase calcium levels in blood
- promotes calcium absorption in the intestines
- reduces calcium storage in bone and calcium excretion in urine
Adrenal glands
3 corticosteroids release is stimulated by ____?
Sit on top of the kidneys, two distinct areas (similar structure to kidneys):
-
adrenal cortex: secretes steroid hormones corticosteroids
- Release of corticosteroids is stimulated by adrenocorticotropic hormone (ACTH) from anterior pituitary
-
3 corticosteroids
-
glucocortisoids (cortisol): sugar
- cortisol released in response to stress and low blood glucose, also suppresses inflammation
-
mineralocorticoids (aldosterone): influence fluid and salt balance
- aldosterone promotes fluid retention by increasing sodium reuptake
- sex hormones (androgens and estrogens): low level production, moreso in sex organs
-
glucocortisoids (cortisol): sugar
-
medulla: interior region of each gland surrounded by the cortex
- produces amino acid derived horones epinephrine and norepinephrine (catecholamines)
- sympathetic fight or flight
- epinephrine used in Epi-Pens to treat anaphylaxis
- sympathetic fight or flight
- produces amino acid derived horones epinephrine and norepinephrine (catecholamines)
Pancreas and 3 cell types
Located posterior to the stomach
Produces hormones important for metabolism, bridge b/w endocrine and digestive systems
- specialized cell types each release diff hormones
-
alpha cells: release glucogon in response to low blood sugar
- promoting catabolism via gluconeogenesis and glycogenolysis
- Beta cells: release insulin, opposes effects of glucagon by promoting glucose uptake in body tissues
-
Delta cells: secretes somatostatin (growth-hormone inhibiting hormone)
- reduces stomach acid secretion and blocks release of other digestive hormones to slow digestion
-
alpha cells: release glucogon in response to low blood sugar
Reproductive organ hormones
Testes and Ovaries
Respond to LH and FSH from anterior pituitary to release testosterone in males and estrogen in women, help develop secondary sex characteristics
Secondary Endocrine Organ - Pineal Gland
Small structure near brain stem: secretes melatonin
- regulates sleep cycles and wakefulness
- sold OTC for insomnia
Secondary Endocrine structures - the heart’s hormone
Atrial Natriuretic Peptide: produced by muscle cells in the heart, helps regulate fluid balance like aldosterone and anti-diuretic hormone but opposite effect
- released in response to high blood volume
- decreases blood pressure by promoting fluid loss
Immune system endocrine organ and function
Thymus- secretes thymosin, hormone that helps T cells develop and mature
Digestive endocrine hormones
Gastrin
Secretin
Cholecystokinen (CCK)
6 key endocrine (hormonal) processes:
Blood glucose
Blood calcium
Stress
Fluid balance
Metabolic rate
Sexual development
Blood glucose regulation
Hormones with effects
Normal blood glucose range : 70 mg/dL to 140 mg/dL
- too little = tissues starved
- too much = glucose not being stored and physiological consequences
Insulin- produced by beta cells in pancreas in response to elevated glucose levels (i.e. after a meal)
- once released, binds to receptors on wide range of target cells mobilizing the cells glucose transporters, lowering conc of glucose in the blood
Glucagon- produced by pancreatic alpha cells when blood glucose levels are too low
- increases glycogenolysis and gluconeogenesis, which liberate glucose and result in high blood sugar
Glucose and insulin also affect protein and lipid metabolism
Cortisol (glucocorticoid released by adrenal cortex): increases blood glucose in fasting state by activating gluconeogenesis and glycogenolysis in the liver
Epinephrine (adrenal medulla): raises blood sugar by stimulating glycogenolysis in liver and muscle cells; fight or flight response
Growth hormone: increases blood glucose under intense physical stress or periods of growth and development
Endocrine calcium regulation in the body
hormones
Necessary for proper bone development, muscle contraction, signal transduction
- travels through the bloodstream and body must maintain specific levels
Parathyroid Hormone (PTH): parathyroid gland secretes PTH when calcium levels get too low
- stimulates bone resorpotion*; osteoclasts break down bone and release calcium
Calcitonin (opposes PTH): released by thyroid gland in response to high calcium levels, inhibits osteoclasts
Vitaman D (D2, D3)
-
Calcitriol: hormonally active form that regulates calcium homeostasis
- increases serum calcium levels by promoting calcium absorption from GI tract, reducing secretion in urine and activating osteoclasts
Endocrine maintenance of fluid levels
Two problematic systems:
Blood volume and omsolality in vascular system
- Too much fluid raises blood pressure: more pressure, solutes more dilute = lower blood osmolality
2. Too little fluid lowers blood pressure: less fluid available to exert pressure on vessel walls; amount of solute stays constant blood osmolality is high
Renin-angiotensin-aldosterone system (RAAS)
Juxtaglomerular cells of kidney sense a decrease in fluid levels and release an enzyme called renin
- Renin cleaves angiotensinogen, inactive protein from the liver
- liberates angiotensin I
Then, in the lungs, angiotensin-converting enzyme (ACE) converts angiotensin I into angiotensin II
- angiotensin II travels to adrenal cortex and simulates aldosterone release, increases fluid retention and blood pressure
- promotes reabsorption of ions in the nephron (kidney)
As blood pressure increases, kidney stops producing renin (negative feedback)
RAAS Dysregulation
RAAS can become pathologic when dysregulated
- excess aldosterone can cause dangerous increases in BP
ACE inhibitors: treatment for high BP
Maintenance of BP and fluid levels: hormones for low BP
Aldosterone and Antidiuretic hormone (aka vasopressin): fluid retention increases, blood pressure increases (through different mechanisms):
aldosterone: secreted by adrenal cortex in response to low blood pressure
- regulated by Renin-angiotensin-aldosterone system (RAAS)
- promotes Na reabsorption, maintains osmolality
antidiuretic hormone (vasopressin): secreted by posterior pituitary in response to low BP and high plasma osmolality
- increases the permeability of kidneys collecting duct to water
- initially reduces blood osmolality
Maintenance of fluid levels: hormone when BP is too high
Opposite of
Atrial Natriuretic Peptide (ANP): produced by cardiomyocytes (muscle cells of the heart); released in response to high blood volume
- opposite of aldosterone and vasopressin (ADH)
- decreases sodium absorption in distal tubule and collecting duct of kidney
- increases filtration rate in glomerulus
- inhibits aldosterone release
Decreases blood pressure by promoting fluid loss
Endocrine regulation of stress (short term and long term)
Short-term(acute) stress: fight or flight response
-
epinephrine and norepinephrine: catecholamin hormones from amino acid tyrosine; released by adrenal medulla
- released in response to sympathetic NS
- increase blood glucose, heart and breathing rates, pupil dilation, blood diversion
Long-term(chronic) stress: repeated exposure to stress
-
cortisol: increases blood glucose by stimulating gluconeogenesis (opposes insulin)
- suppresses inflammation
- deleterious long term effects
Endocrine regulation of metabolic rate:
2 hormones
Thyroid hormones T3 and T4 released in respond to Thyroid Stimulating Hormone (TSH), which is released by anterior pituitary
T4: four iodine atoms, precursor to T3
T3: 3 iodine atoms
- 3-4 times more potent than T4
Insufficient levels lead to hypothyroidism: fatigue, cold intolerance, weight gain, depressed heart/respiratory rates
hyperthyroidism: weight loss, increased appetite, rapid heart rate
Endocrine regulation of sexual development and puberty
LH, testosterone and estrogen
During fetal development, presence of androgen hormones –> development of male/female traits
- then, sex hormones have little effect until hypothalamus-driven surge of hormones called puberty
- pulses of gonadotropin-releasing hormone (GnRH) stimulate anterior pituitary to release leutinizing hormone LH and follicle stimulating hormone (FSH)
Females: In response to leutinizing hormone (LH) and FSH, ovaries produce more estrogen and progesterone
- initiate and regulate the menstrual cycle
- promote development of female secondary sex traits (enlarged breasts, widened hips)
Males: LH and FSH act on testes to trigger release of downstream hormones
- LH causes Leydig cells of testes to produce testosterone
- Testosterone contributes to male secondary sex traits like facial hair and voice deepening
- FSH affects Sertoli cells, trigger the release of factors for sperm maturation
Estrogens and Androgens
What are primary and secondary sex characteristics?
Classes of Hormones; both produced in males and females but at varying levels
- Estrogen: estradiols, progesterone
- Androgen: testosterone
Primary traits: reproductive organs (penis, testes, ovaries)
Secondary traits: changes in fat distribution, hip widening, growth of breast in females; facial hair and deeper voice in males
Sex hormones in adulthood
Menopause
Females: estrogen and progesterone regulate menstrual cycle; if pregnancy occurs, levels continue to rise
- at beginning of pregnancy, both produced in corpus luteum (formed by ruptured follicle cells) in the ovaries
- later, taken over by placenta, which also produces Human Chorionic Gonadotropin (hCG)
- produced in placenta and maintains corpus luteum during pregancy (detected on pregnancy tests)
- later, taken over by placenta, which also produces Human Chorionic Gonadotropin (hCG)
- oxytocin in childbirth
Throughout aging, sex hormones produced less but much more abrupt in females
Menopause: typically occurs in 40s or 50s, plunging sex hormone levels and cessation of menstruation
- hot flashes, night sweats
Sex hormones in medicine
Hormonal contraceptives, hormone replacement therapy
- synthetic hormones
- prevent pregnancy or mitigate menopause
- polycystic ovary syndrome
- facilitate secondary sex characteristics in transgenders
Estrogen is produced by
Ovarian follicle cells, corpus luteum formed from ruptured follicle cells, and placenta
(anterior pituitary forms GnRH which leads to production of estrogen)
Menstrual Cycle in females
3 main parts:
Hormonal and physiological changes in reproductive tract
- 28 day interval, beginning in puberty ending in menopause
1. Ovarian Cycle- 3 phases all in ovary all to release ovum
- Follicular phase- follicle matures
- Ovulaton- egg released
-
Luteal phase- after ovum is released, follicle is transformed into corpus luteum
- if pregnancy doesn’t occur, corpus luteum decays
2. Uterine cycle- uterus preparing for the ovum
-
Menses/menstruation: same time as follicular phase, uterine endometrium thins as tissue buildup in previous cycle is sloughed off
- typically 3-5 days but variation
- Proliferative phase: Once menses is complete, uterine endometrium thickens/enriches with blood vessels
- Secretory phase (during luteal phase): Lining continues to thicken and if ovum is fertilized and implants pregnancy begins
3. Hormone regulation:
At beginning of follicular phase, increase in FSH that induces follicular development; estrogen levels rise to stimulate endometrium development
- Rare estrogen positive feedback on hypothalamus that stimulates brief surge in LH and FSH –> triggers ovulation
- causes ruptured follicle to form corpus luteum
In the luteal phase, corpus luteum secretes high levels of progesterone which help maintain endometrium readiness for implantation
How does body know that implantation has occured?
If body didn’t know implantation had occured, embryo would be destroyed during menstruation
In the absence of implantation, negative feedback loops keep menstrual cycle moving forward
- corpus luteum usually responds to LH but progesterone (secreted by luteum) inhibits LH, causing corpus luteum to degrade
If implantation occurs, embryo secretes Human Chorionic Gonadotropin (HCG) which maintains corpus luteum
- continues producing progesterone, maintains uterine endometrium
- then progesterone levels taken over by placenta
Oxidation reduction reactions
One atom gains electrons, another atom loses them on (on same side of eqn)
- not just trading out substituents
OIL RIG
All atoms have an oxidation state based on position on periodic table
- losing electrons increases charge, oxidation state increases = oxidized
Reduction- when reduced, oxidation state is lowered (from 0 charge to -2)
- gain of bonds to hydrogen, loss of bonds to EN atoms like oxygen
Oxidation- gaining electrons is being reduced, losing them is being oxidized
- losing bonds to H, gaining bonds to O

Oxidizing and Reducing agents
Species that is reduced (loss of charge/gain of electrons) = oxidizing agents
- Often contain Cr, O, or other EN element
- Na2Cr2O7 - sodium dichromate
- CrO3 - chromium trioxide
- PCC
- weak oxidizing agent
Species that is oxidized (gain in charge/loss of electrons) = reducing agent
- NaBH4 -weak
- LiAlH4 strong
Usually talking about specific compounds you can add to a mixture to reduce or oxidize another compound
Oxidation States
All atoms have different electronegativity and share electrons unequally
- complete in the case of ionic bonds
- partial in polar covalent
- minimal in nonpolary covalent
Assigning oxidation states:
- Pure elements are 0 - H2, O2, F2, N2, Na, Fe
- Monoatomic ions equal to their charge
- Fe2+ = +2, Cl- = -1
- Sum of oxidation states is equal to overall charge of compound
- F is always -1, halogens are -1 unless bonded to more EN halogen, N, or O
- H is +1 unless bonded to more electropositive element (then its -1)
- Oxygen is -2 unless its a peroxide (-1)
- Alkali metals always +1 (like hydrogen), alkaline earth metals always +2
Go through functional groups for larger compounds
**oxidation state of carbon can vary dramatically
Redox rxns are usually what type of reactions?
Metabolic processes that are redox reactions?
Single displacement - free elements have oxidation state of 0, can change when bonded in a compound
Combustion - hydrocarbon + oxygen = CO2 + water
Combination - A + B –> AB
- Glycolysis- NAD+ reduced, multiple C=O double bonds created
- Citric acid cycle, electron transport chain
- Beta-oxidation

Balancing Redox Reactions (half reactions)
Neglect elements not being oxidized or reduced
- write half reactions, one for reduction of element and one for oxidation of element
- Assign oxidation states
- Balance half reactions (except oxygen and hydrogen)
- Balance oxygen by adding H2O
- In acidic conditions, balance eqn by adding H+
- in basic conditions, add H+ then equal amounts of OH on both sides, combining them to make H2O and cancelling out
- Add electrons to balance charge
- Multiply both half equations to make electrons equal on both sides
- Combine half reactions and cancel

Redox titrations
Colorimetric indicator that indicates when oxidation/reduction has occured - usually use manganese
- permanganate ion is purple, manganese cation is colorless
Att equivalence point, reaction turns purple, no more reactant to be oxidized or reduced
- number of moles equal (e donated by one and absorbed by the other)
Normality of redox rxns: instead of [H+] and [OH-] conc, use the number of e’s gained or lost (picture) as “n”
n1M1V1 = n2M2V2

Standard Reduction Potential
Tendencies for atoms to be reduced in any redox reduction half reaction (E°)
- measured in volts, relative to each other
- the more positive an E° is, the more spontaneous the reduction
- the more negative, the more nonspontaneous the reduction
**Any half reaction can be reversed to form the oxidation half rxn, reaction that is more spontaneous ISNT reversed
- also reverse sign of E°
- add two potentials for standard potential of full rxn
Don’t need to balance eqn, not affected by stoichiometric constants

Electrochemical cells
Two types of electrochemical cells
Electrochemical cells: a device set up to harness a redox reaction to generate or use electrical energy
- all have anode - oxidation half reaction
- and cathode - reduction half reaction
Galvanic and electrolytic cells
***Electrons move from anode and are liberated via oxidation to the cathode, where they reduce the species in solution
Galvanic Cells
A spontaneous redox reaction is used to generate a positive potential difference that drives a current
- Standard Reduction Potential (E°) is always positive (spontaneous rxn)
Anode and cathode consist of metals used in half reactions (grow and shrink)
To calculate direction of spontaneous reaction:
- Identify which half reaction has higher reduction potential, this will be the CATHODE SIDE
- Other half reaction will be ANODE which is the site of oxidation
- FLIP the anode half reaction and its sign
- Left with reduction and oxidation potential, which you can add to get E° (if this is negative, its incorrect)

Daniell Cell
Galvanic cell example - cathode and anode half reactions are separated
Anode and cathode half cells connected by conductive wire and by a salt bridge: allows ions not participating in redox to travel from one solution to another
- these ions equalize the charge that is changed by the conductive wire (anode becoming more positive & vice versa)

Concentration cell (galvanic cell)
Cathode and anode half reactions aren’t physically separated
Electrodes are same material
Two different molar concentrations

Electrolytic cells
Energy put into system to drive a nonspontaneous redox rxn = negative Ecell values
- name electrolytic infers these reactions are often to break down compounds into parts with electrical energy
- ex. 2H2O –> 2 H2 + O2
Two electrodes: ***anode (+) and cathode(-) (usually just conductive metal)
- BECAUSE ANODE IS + AND CATHODE IS -, REQUIRES ENERGY TO PUSH ELECTRONS
- Hydrogen produced at cathode (site of reduction, H is reduced from +1 to 0)
- Anode is still oxidation site, this is where oxygen is produced
Same reactions can be used for both cell types, **But net reaction and sign will be flipped

Electroplating
Rechargeable batteries
Use both galvanic and electrolytic cells
- can either discharge spontaneously(galvanic) or recharge (electrolytic)
Lead acid battery- low energy to mass ratio (bulky battery), still used today
- in charged state, has PbO2 electrode and Pb electrode in acid solution
- reactions are flipped for charge and discharge
Nickel cadmium battery

What does Nernst Equation help with?
Tells us how electric potential of a cell is affected by real world conditions, temperature and concentration of reactants
E’cell = E°cell - RT/zF (lnQ)
Q is inversely proportional, when [products] goes up, electric potential goes down (less spontaneous)

Fluid definition
Any substance that can change its shape to match that of container
- **gases and liquids are fluids
Density (p)
what is the density of water
p = m/v [kg/m3]
g/cm3 = g/mL (1L = 1000cm3)
density of water is 1 g/mL at 4°C and 1atm
Specific gravity
Density of a liquid relative to water; unitless (ratio)
Specific gravity= p(Water)/ p(liquid)
- useful for modeling buoyancy
Pressure equation
SI unit of pressure
PSI units
how do mmHg units work?
atm =
P = F / A [N/m2] = Pascal (Pa) = SI unit
Same force on a very small area is how knives cut things
PSI= pounds per square inch, same as Pascals but non metric: [lbs/in2]
mmHg is measuring pressure difference between two fluids by using difference in height of mercury in U shaped container
atm = average pressure exerted by atmosphere at sea level = 1 atm
Remember:
1 atm = 101,000 Pa = 760 mmHg** = 14.7 psi = 760 Torr = 1 bar
Hydrostatic pressure
Pressure exerted on an object submerged in fluid
- Psub = p gh
= (density of fluid) x (acceleration due to gravit) x (height of fluid above object)
Absolute pressure
Pressure of a liquid on an object as well as atmospheric pressure above it
Pabsolute = Patmospheric + Phydrostatic
*atmospheric pressure is higher at lower altitude
Gauge Pressure
When measuring pressure (like blood pressure, tire pressure)
Pgauge = Psystem - Patmospheric
Buoyancy
Buoyant Force
Whether something floats or sinks in fluid
- degree to which an object is submerged in water is proportional to its specific gravity (density relative to water)
If an object has a specific gravity of .92 (like ice), 92% of the object will be submerged in water
%submerged = pobject / Pliquid x 100
Buoyant force (exerted by water upwards on object)= pVg
- p = density of water
- V = volume of object
- buoyant force is proportional to volume of displaced water

Pascal’s Law
A change in pressure at any location in an enclosed fluid is transmitted equally to all points throughout fluid
- how hydraulic lifts work
F1/A1 = F2/A2
If A2 is greater, F1 is smaller

Surface Tension
Equation
Why does a liquid hold together? presence of intermolecular forces (like H-bonding in water)
In middle of water, each molecule has same amount of attractive forces on all sides
-
Surface tension: **at the interface between air and water at the surface, the water molecules forces act unevenly on the ones at the surface and has no interactions with the air molecules
- this imbalance of forces creates tension
Surface tension = Force / Length (N/m)
- Systems want to minimize surface tension because it has higher energy
- this is why like dissolves like and raindrops fall in their shape
Cohesion forces
Adhesion forces
Meniscus
Effect of intermolecular forces within a given substance causing them to stick together
Adhesion forces are molecules sticking to another type of molecule
- if adhesive forces are stronger than surface tension forces, liquid will crawl up walls of container and surface is curved (concave)
- if fluid acts more strongly with itself than walls of container, has a convex shape
Capillary Action
With a narrow enough tube so that adhesion forces are much greater than surface tension, can get liquid to rise up the tube in opposition to gravity
- how plants utilize water, thin layer chromatography
Study of how fluids flow
Viscosity
Laminar Flow vs Turbulent Flow
Fluid dynamics
Viscosity: liquids resistance to flow (Pa x sec) (pressure x time)
- all fluids are viscous
- decreases as temperature increases
- releases energy
Laminar Flow: flowing fluid composed of parallel layers that may be moving at different velocities
Turbulent flow: flowing fluid composed of mixed layers that vary in pressure and speed
- the higher the velocity, the more likely the flow is to become turbulent
Poiseuille’s Law
Flow rate = ∆pressure drop and radius over length
- large pressure drop causes flow rate to increase
- increasing radius dramatically increases flow right
Bernoulli’s Law (fluids)
**when theres a change in height of container
Highly Idealized fluids- assume laminar flow, neglect viscosity and interactions between the fluid and container
P1 + 1/2pv12 + pgh1 = P2 + 1/2pv22 + pgh2
Energy in 3 forms: Pressure exerted on walls of container, Kinetic energy and potential energy in equation
** at a constant height, increasing velocity will decrease pressure exerted on container
Continuity Equation (fluids)
relates to what biological process
Within a closed system, the flow rate of a liquid constant;
Fluids are incompressible, flow rates must be equal in a closed system
- Q1 = Q2
Since Q = vA
- v1A1 = v2A2
Relates to blood flow in circulation; Q in aorta will be equal to Q in the capillaries as a whole, which will have slower velocity but much higher surface area
Venturi Effect
The narrower the tube, the lower the pressure
(look more into this)

Periodic Motion
amplitude
period and frequency
Object is displaced relative to a midpoint in both the forward and backward directions - pendulum
- if it weren’t for friction and air resistance, motion would be continuous
Amplitude: displacement in (+) and (-) direction from midpoint; values are equal (|A|)
Period (T): time interval motion repeats
Frequency (f): how frequently motion occurs
- 1/T (s-1) Hertz
Forms a sinuisodal curve on a graph
- being out of phase: same frequency and amplitude but not synced up

Cycle of Periodic Motion
Two basic components
Periodic motion involves constant interchange between…
Inertia: an object in motion tends to stay in motion
Restoring Force: brings the object back to its equilibrium
- for a pendulum, this is gravity
Constant interchange between kinetic energy and potential energy (mgh)
- at midpoint, KE is maximized and PE = 0
- at extremes KE = 0 and PE is maxed
Springs (Hookes Law)
Displacement is horizontal, spring oscillates back and forth
Hooke’s Law: F = kx
k = spring constant
x = displacement
If F= -kx, F is referring to the restoring force
Pendulum and springs period equation
Pendulum:
T = 2π √ (L/g)
L = length, g = gravity
Springs:
T = 2π √ (m/k)
Waves are
2 types of waves:
Periodic motion that propagates through space
Mechanical and Electromagnetic waves
mechanical: physical piece of mass that moves back and forth
- pendulum, spring
Electromagnetic waves: oscillating electromagnetic fields
- light
Two types of mechanical waves:
Depends on direction particles are displaced, parallel or perpendicular to the direction of the wave
Transverse: physical components of wave move vertically, while wave moves horizontally (perpendicular)
- wavelength (λ): distance between peaks or troughs
- light
Longitudinal: particles propagate parallel to direction of wave (pushing and pulling motion)
- compression waves
- amplitude = level of compression
- sound waves

Velocity of waves is affected by…
Velocity of wave eqn
The medium it propagates through
v = λf
- m/s = m/s2 (s-1)
Wave interference
When waves overlapm, they create a new wave with amplitude equal to the sum of their original amplitudes
Constructive interference: amplitudes align (are pointed in same direction), new wave has greater magnitude
Destructive interference: waves cancel each other out

Standing waves
examples
Many waves overlapping and interfering with each other in a consistent manner
When graphed, sinuisodal graph with points of no displacement = nodes
Antinodes: points of maximum displacement
- 1 λ = 2 antinodes
Resonance frequency: object’s natural vibration frequency enabling maximum amplitude
Examples:
pipes and strings
Harmonics of strings
1st harmonic: Standing wave on a string with only one antinode is lowest frequency
- wavelength is twice the length of string (1 wavelength is two antinodes)
2nd harmonic: two antinodes, wavelength = length of string
3rd harmonic: 3 antinodes, 1.5 wavelengths
λ = 2L / N

Standing waves and pipes
Each end of pipe can be either closed or opened - closed ends have a node
- open ends have an antinode
If a pipe is open at both ends, has two antinodes
- can use same equations as those used for a string attached at both ends (harmonics)
** N = nodes instead of antinodes with strings
** come back to this video
Gibbs Free Energy (∆G)
∆G° = standard free energy
Amount of energy available in a system that can be used for work on its surroundings
- ∆G indicates how spontaneous a reaction will be
- (-): spontaneous and exergonic
- (+): nonspontaneous and endergonic
∆G° = free energy at 273.15 K, 1 atm, 1 molar conditions
∆G = ∆G° + RT lnQ
** In non spontaneous biological reactions, pathway will shunt out product so that reaction shifts towards making more product

Coupling Reactions (additivity)***
commonn biological mechanism
Coupling with nonspontaneous (endergonic reactions) with spontaneous (exergonic) to drive nonspontaneous rxns forward
- product of endergonic reaction is the reactant of exergonic (intermediate)
- pulls out product quickly so that reaction is driven forward
Add ∆G values for each to obtain free energy of entire process
- **if overall ∆G is negative, whole process is spontaneous
Common mechanism:
Powering nonspontaneous reactions via ATP hydrolysis (HIGHLY spontaneous)

4 basic forces of nature and why protons stick together and don’t attract its electrons
4 Basic Forces of Nature:
- electromagnetic
- gravitational
- strong nuclear
- weak nuclear
Strong nuclear force: holds protons together in the nucleus, stronger than the electromagnetic force that would normally drive them apart
- in this bound state, protons are more stable, energy difference is dissipated by nuclear binding energy
Mass Defect (binding energy and mass)
Relationship between binding energy and defect
Binding energy and mass: MASS DEFECT of an atom: mass of a nucleus is less than that of its individual constituents
- small amount of mass is transformed into binding energy
When nucleus dissassembles into smaller units, the binding energy is amount of energy input required
E = MC2
binding energy = mass (speed of light)2
- all objects with mass have energy
- m = mass defect (difference between unit mass and individual constituent mass)
This is the energy associated with nuclear power, binding and splitting atoms
Why are protons and electrons not attracted to each other within an atom?
Electrons have particle and wave-like properties (like all matter);
λ = h / mv
h = planck’s constant (6.62 x 10-34 Jxs)
Photoelectric effect (einstein)
Light shone on a metal surface causes electrons to be emitted from the metal
- when photons hit the surface of a metal, excite metallic electrons to higher energy states and move further from their nucleus, eventually ejecting from their atoms
Requires energy = Work Function (Φ)
- incident photon has to have at least the energy of the work function to emit an electron
- Ekinetic = hf - Φ
KE = plancks constant x freq of light - (work function)
- kinetic energy of the electron emitted is the leftover energy past the threshold of the work function
isotopes
Isotopes: atoms with same number of protons but different number of neutrons
Nuclear reactions
4 types to know
Any reaction involving particles in the nucleus
- Fusion
- Fission
- Nuclear Decay
- Transmutation- the reverse of nuclear decay, only in lab settings
Nuclear fusion
Two or more nuclei are forced together by extremely high levels of energy(like the sun), causing them to merge into new larger nucleus
- releases a lot of energy due to dissipation of binding energy of larger nucleus
- produces a neutron

Nuclear fission
Large nucleus split into 2 or more nuclei
- no nuclear particles lost
Radioactive decay
3 types
Unstable isotopes break down and eject mass, energy or photons
-
Alpha decay- emission of an alpha particle (2 protons and 2 neutrons)
- decrease in atomic number by 2 and atomic mass by 4
- emitted particles interact with matter and can be dangerous to tissue
- can be easily shielded against and don’t break skin or clothing
- emitted particles interact with matter and can be dangerous to tissue
- decrease in atomic number by 2 and atomic mass by 4
-
Beta Decay- 2 forms
-
Beta minus: neutron converted to proton and electron is ejected
- atomic number increases, mass doesn’t change
-
Beta plus: proton converted to neutron and positron is ejected
- atomic number decreases, mass doesn’t change
-
Beta minus: neutron converted to proton and electron is ejected
-
gamma decay
-
emission of high energy photon (gamma ray) from an excited nucleus
- gamma rays have no mass or charge
-
emission of high energy photon (gamma ray) from an excited nucleus
Electron capture
Nucleus absorbs an electron which merges with a proton to form a neutron
- atomic number decreases, weight unchanged
Electron + proton = neutron
Half-life
Timing of radioactive decay so predictable can be used to determine age of rocks and artifacts (carbon dating)
Half life- amount of time for half of existing material to decay
- ex. every 5 miniutes, half of the existing material decays
Nt = N0(1/2)t/t1/2
amount of radioactive material at time (t) equals original amount times .5 to the power of half lives that have passed; if half life is 2 years, after two years = .52