Lecture Exam 1 Flashcards
Emergent Properties (5)
Levels of Structural Organization:
trait or characteristic possessed by an object due to the arrangement and interaction of its components; property is not found in the components themselves
“eat” Energy utilization
“sleep” Homeostasis
“grow” Growth and development
“repeat” Reproduce (transition of genetic material)
“Evolve”
Possess high level of structural [O]rganization
Life consists of [C]ells
Levels of Structural Organization (big to small): organ systems > organs > tissue > cells > organelles > surpramolecular systems > macromolecules > molecules > atoms
Properties of Water (5)
- Has polar molecules that have a high propensity for forming hydrogen bonds, thus creating a dynamic crystalline lattice
- High degree of cohesion due to H bonding
- High specific heat
- High heat of vaporization
- Important solvent that can dissolve polar or charged molecules
Element Information to Know
92 naturally occurring elements, 25 of which can be found in organisms
4 main players → C, H, O, N ⇒ specifically (by mass) 63% O + 25% C + 9% H + 5% N = 97% total
(( Remaining 3% are the other 21 naturally occurring elements))
Carbon = key player bc can form FOUR covalent bonds and long carbon chains, thus becoming the backbone of biomolecules
Functional Groups to Know
- Hydroxyl
- Carbonyl
- Carboxyl
- Carboxylic Acid
- Amino
- Amine
- Sulfhydryl
- Thiol
- Phosphate
- Methyl
- Acetyl
Hydroxyl = R-OH
Carbonyl = R-CO-R
Carboxyl = hydroxyl and carbonyl together → R-CO-OH; also known as “COOH”
Carboxylic acid = molecules w/ carboxyl group
Amino = R-NH2
Amine = compound w/ N, ammonia derivative → eg. N-R3 where R can vary and be different from one another
Sulfhydryl = R-SH
Thiol = compound w/ “sulfhydryl” func group
Phosphate = R-PO4 -2
Methyl = R-CH3
Acetyl = carbonyl + methyl; R-CO-CH3
Define the following:
- Isotopes
- Isomers
- Structural Isomer
- Sterioisomer
ISOTOPES: compounds with the same number of protons (thus same chemical identity) but different number of neutrons (thus have different atomic masses); will have keep approximately the same chemical properties
ISOMER: same molecular formula but different structures; result in different properties (eg. melting point)
STRUCTURAL ISOMER: different bonding
STEREOISOMER: retain same boding, diff spatial arrangement → enantiomer (all mirror) and diastereomer (at least one non mirror)
Explain how to determine the following:
- Number of Stereoisomers
- D or L conformation
- R or S configuration
How to find number of stereoisomers:
Find asymmetric carbons
Number of stereoisomers: 2n where n is the number of asymmetric carbons
– Number of pairs of enantiomers: (2n) / 2 where n is the number of asymmetric carbons
How to determine D or L conformation?
Look at asymmetric carbon that happens to be farthest from the carbonyl group
– If hydroxyl group is to the LEFT, then will be L → living systems only have L
– If to the RIGHT, then will be D
How to determine R or S configuration?
- Number the priority groups
- Look at 1 > 2 > 3
- - If CLOCKWISE, then S → running out of time [S]ucks on exams
- - If COUNTER-CLOCKWISE, then R → if only I could [R]ewind the time!
Define the following:
- Biomolecules
- Macromolecules
- Disaccharide
- Oligosaccharide
- D-n-Acetylgulcosamine
BIOMOLECULES: carbohydrates, proteins, nucleic acids, lipids → all but lipids are polymers, aka macromolecule with repeating units of monomers
MACROMOLECULES: constructed by forming covalent bonds between building blocks, called linkages which are formed by the removal of H2O (aka dehydration or condensation reaction); can be reversed by hydrolysis (which adds water into the linkage to break it and reform the hydroxyl groups
DISACCHARIDE: 2 monosaccharides joined by covalent bond; used in transport via dehydration reaction
OLIGOSACCHARIDE: contains three to twenty monosacharrides; involved in cell communication and identification; can be found on the surface of the cell membrane (configuration of which results in different blood types)
D-n-acetylglucosamine: located in chitin and made from derived monosaccharides; can be found in skin and cartilage
Classification of Monosaccharides (2)
By location of carbonyl: basically, where is the C=O bond?
- Aldose: on one end of the linear chain → -CHO end
- Ketone: internal location within the linear chain
By number of carbons: ie. C3 = trioses; C4 = tetroses
– Under physiological conditions, glucose (and other hexoses / pentoses) exist as CLOSED RINGS as equilibrium favors the ring formation more than the linear
Functions of Carbohydrates (aka simple sugars) + Formula
monomer as basic building block
Formula: (CH2O)x where x is between 3 and 7 → when numbering, start at the end closest to the carbonyl grou
- Raw material for biosynthesis + fuel for cellular respiration
- Monosaccharide derivatives: just replace hydroxyl
- - Acid sugars: change to carboxyl → C-OOH
- - Amino sugars: change to amine → C-NH2
Types of Polysaccharides (2)
STORAGE polysaccharides: storing carbohydrates / fuel used in respiration; considered as “quick use” → Starch: three sub types
- Amylose: linear polymer of glucose
- Amylopectin: branching polymer of glucose
- Glycogen
- All three are polymer in glucose ! Have a (loose) spiral form in order to interact with water.
STRUCTURAL polysaccharides are not for quick use (unlike storage); usually form some part of the organism’s structure → Cellulose
Alpha and Beta Configuration
- Determination
- Digestion
- Identify the anomeric carbon.
- Counting begins from the anomeric carbon if there is not a CHO group attached; otherwise, the anomeric will count as the second carbon while the C in the CHO group will count as the first.
- Look at the carbon in the ring that is farthest from the anomeric carbon. Determine R or S configuration.
- IF R CONFIGURATION, return to the anomeric carbon and look at the OH group that is attached. (Invert if S configuration)
– If below the plane, then ALPHA → alpha looks like a fish and fish live in the sea (below ground)
– If above the plane, then BETA → beta starts with b and so do birds, live in the sky (above ground) - For glycosidic linkages: one of the linkages will come from an anomeric carbon. Use this to orient yourself.
If two anomeric carbons are involved, start with the one of the lower numbering.
** BE AWARE OF FLIPS.
Animals can DIGEST only starch and glycogen BUT not cellulose despite all three being polymers of glucose.
- Difference lies in the configuration of ring formation (thereby affects the animal’s ability to digest cellulose)
- Alpha configuration for starch and glycogen
- Beta configuration for cellulose
Define the following:
- ProteinS
- Chaperone proteins
- Conformation
What affects conformation?
PROTEINS: 50% dry weight; amino acids as monomers; function depends on conformation
– Structure: NCC backbone = central carbon atom with four bonds → hydrogen, carboxylic acid (COOH), amino (NH2), and R (side chain)
CHAPERONE PROTEINS: assist in the folding / refolding of a protein into the proper conformation
CONFORMATION: easy to change because of “sliding” motion → contrast to configuration, which is rigid and hard to change
What affects conformation?
- Aka denaturation, specifically due to changes in temperature or pH
- Increased temperatures = increased thermal vibration, which can overcome weak H+ bonds → contrast to low temperatures that lower the kinetic energy so much that no collisions (and therefore no reactions) occur
- Low pH = excess H+ ions, which can disturb the ionic interactions or neutralize the charge on negatively charged R groups
Four Types of Protein Structures
PRIMARY: aka native conformation bc determined by DNA; linear sequence of amino acids in the polypeptide chain
SECONDARY: localized areas of folding stabilized by H bonding btwn double bonded O carbonyl (formerly carboxyl end) of one amino acid and the -H on the amino end of another amino acid
- Alpha helix: most abundant secondary structure in proteins
- Beta pleated sheet: also localized but does not cover the entire polypeptide
TERTIARY: global folding with interactions between the R groups (ie. hydrogen bonds, ionic bonds, disulfide bridges), thereby generating a three dimensional structure
– Hydrophobic interactions: water-soluble proteins have a hydrophobic core in which side chains are buried from water, which stabilizes the folded state; charged and polar side chains are situated on the solvent-exposed surface where they interact with surrounding water molecules
QUARTERNARY: more than one polypeptide and their interactions
Define the following:
- Lipids
- Fats
- Phospholipids
LIPIDS: once again, not a polymer; Hydrophobic; uses a 3 carbon chain called GLYCEROL as its basic building block
– Each carbon has a hydroxyl; empty spaces are hydrogens.
FATS: aka macromolecule; glycerol and 3 fatty acids that are linked by ester linkages (involves dehydration reaction)
- Maximum number of fatty acids is 3 (triglyceride) but di/mono also exist.
- Function: long term storage of energy; cushioning / protection; insulation
PHOSPHOLIPIDS: type of fat; in water, forms as micelles, liposomes, and bilayers (spontaenous formation)
– Replace one fatty acid with a phosphate and a polar molecule → hydrophilic head with long hydrophobic tail
Fatty Acids
- Structure
- Naming (2)
STRUCTURE: HOOC - (CH2)x - CH3 → carbonyl - variable amounts of CH2 - methyl
Saturated: full amount of H bc no C=C bonds → tend to be solid at room temperature bc pack together easily
Unsaturated: contains C=C bonds (more than one = polyunsaturated); can be cis or trans → cis introduces a kink, making them oils at room temperature
NAMING: ratio of number of total carbons to number of C=C double bonds
- Biochemist naming: aka alpha naming system; begins at the CARBOXYL END → attaches Δ #s to denote the location of the double bond STARTING FROM THE CARBOXYL END
- Dietician naming: aka omega naming system; begins at the METHYL END → attaches omega #’s to denote the location of the FIRST double bond STARTING FROM THE CARBOXYL END
Define the following:
- Nucleic acids
- Nucleoside
- Polynucleotide
- other nucleic acid / nucleotide derivatives
NUCLEIC ACIDS: nucleotide as monomer → composed of a phosphate (attached to carbon 5), a 5 carbon sugar, and a nitrogen base (attached to carbon 1) that are linked together by phosphodiester linkages!
- Nitrogen base: organic ring which can be singular as a pyrimidine (for C, T, U) or doubled as a purine (A, G)
- DNA: Adenine, Cytosine, Guanine, Thymine → no U for uracil
- RNA: A, C, G, U → no T for thymine
NUCLEOSIDE: nucleotide minus the phosphate group
POLYNUCLEOTIDE: linear polymer whose molecule is composed of many nucleotides units (usually 13 or more); ie. DNA or RNA
OTHER nucleic acids / nucleotide derivatives:
- Energy carrier as ATP
- Coenzymes: entities added to enzymes; vital for enzyme function → NOT A PROTEIN!
- - Most nucleotide-derived coenzymes function in the energy utilization process → ie. Coenzyme A - Signalling molecules → ie. cAMP
Define the following:
- Cells
- Cell Theory
Compare electron microscopes with light microscopes.
CELLS: basic unit of life; coined by Robert Hooke in 1665 → ideal for a big surface area (production) to volume (consumption) ratio
CELL THEORY: first two are originally from Schleiden and Schwann in 1839
- All organisms consist of cells
- Cells arise from other cells by cell division
- Chemical reactions occur in cells
- Cells contain hereditary material (for reproduction)
Electron microscopes > light microscopes bc use smaller wavelength, therefore has better resolution BUT can only see structural artifacts and thing examined must be dead
What do all cells have? (4)
Compare the two types of cells.
ALL CELLS HAVE:
- Plasma membrane (phospholipid bilayer)
- Genetic material (DNA)
- Cytoplasm
- Enzymes (inside cytoplasm)
TWO TYPES OF CELLS: eukaryotic versus prokaryotic
- PRO = archaea / eubacteria domain; DNA is a single circular molecule with few proteins for packaging; No nucleus with few or no membrane bound organelles; Typically small (1-10um)
- EU = eukarya domain (including protists, fungi, animals, plants); DNA linear chromosomes; Nucleus present with Many membrane bound organelles; Larger → have internal membranes that partition cells into compartments; have unique lipid and protein compositions; created a localized environment for reactions; isolate incompatible reactions; allow for localized or global concentrations
Grams
- Staining Process
- Positive versus Negative
Staining Process:
- Crystal violet staining, followed by light water wash
- Iodine → binding agent for violet, thus making it harder to remove
- Ethanol → dissolves LPS but, if overdone, can overpower the iodine and remove the crystal violet
- Safranin staining (red)
(+) Positive has a thick layer of peptidoglycan, therefore takes up both dyes but primarily shows up as VIOLET → also has 2 basal rings
(-) Negative has a thin layer of peptidoglycan BUT also has a lipopolysaccharide outer membrane, therefore primarily shows up as RED (bc violet-stained LPS dissolved) → also has four basal rings
Endomembrane System (6)
use vesicles to transport things from its lumen to whatever it touches
– Overview: Nucleus creates, ER synthesizes; Golgi modifies and ships out to plasma membrane, lysosomes, or vacuoles
- Plasma membrane: semipermeable bc of phospholipid bilayer; controls traffic in and out of the cell
- Nucleus: surrounded by nuclear envelope (inner AND outer phospholipid bilayer membranes); contains nucleolus (produces ribosomes for use in protein synthesis) and nucleolar organizer (contains genes to make ribosomes; specific sections on chromosomes where the nucleolus can form)
- Endoplasmic reticulum: conglomeration of membranous tubes, the lumen of which is called CISTERNAE
- - Smooth: no ribosomes; synthesis of lipids; carbohydrate metabolism; detoxifies by adding -OH (more polar / water soluble, therefore easier to get rid of); store Ca++ (calcium; used for muscle contraction and neurotransmitter release)
- - Rough: synthesis of secretory / membrane / endomembrane proteins; membrane production; products are shipped to the golgia via transport vesicles - Golgi: modifies, stores, reroutes products of ER; enzymes can alter phospholipids or target products
- - Cis side = facing towards ER; receiving side
- - Trans side = facing away from ER; shipping side - Lysosomes: 40+ hydrolytic enzymes (lipases, carbohydrases, proteases, nucleases); used for intracellular digestion, recycling / autophagy (recycle old organelles vs. starving cell will break down functional organelles for cellular respiration)
- Vacuoles:
- - Food
- - Contractile: stores and excretes waste and excess water by merging with the cell membrane to dump its contents outside the cell; found in protists
- - Central: stores various things; acts like a lysosome sometimes if contains enzymes; can trigger apoptosis (programmed cell death) if contains poison
Cytoskeleton + 3 Types of Fibers
network of proteinaceous fibers throughout the cytoplasm to provide framework and support movement
- Microtubules: largest of the three; originate from the microtubule organizing center; primarily for cilia and flagella
- - hollow fibers made of alpha and beta tubulin
- - Dynein (-) motor and kinesin (+) motor - Microfilaments: smallest of the three
- - Solid rods made of Actin (+/ - ends)
- - Myosin (motor protein) - Intermediate fibers: made of keratin subunits, therefore more permanent (harder to depolymerize as opposed to dimers or actin
Cilia and Flagella (of eukaryotes)
Cilia is shorter than flagella
Both are hair like structures projecting from the plasma membrane that draw fluid across the cell surface, allowing for movement and replacement of stale material
9 outer microtubular DOUBLETS (two microtubules that share a common wall) + 2 central microtubules
– Basal body: 9 peripheral TRIPLETS (three microtubules that share a common wall) with nothing in the middle; acts as an anchor by attaching to the cytoskeleton
Movement is due to the motor proteins dynein and kinesin that allow for “walking”
Define the following:
- Cell wall
Extracellular matrix
CELL WALL:
- Found in plants (cellulose), fungi (chitin, specifically n-acetylglucosamine), bacteria, and most algae
- Basically a rigid, static structure found outside the plasma membrane
- Used for protection, shape, and preventing the excess uptake of water via osmosis (thus preventing the cell from bursting)
EXTRACELLULAR MATRIX:
- (in animals) web of glycoproteins (proteins + carbohydrate), extracellular proteins, and polysaccharides that are associated with the OUTER FACE OF THE MEMBRANE
- Used for support, adhesion, and cell communication / regulation
Fluid Mosaic Model of the Membrane Structure
developed by Sanger and Nicolson in 1972
- Plasma membranes are NOT static.
- Protein associations are stable due to hydrophobic and hydrophilic interactions.
- Fluidity rises from the lateral drift of lipids / proteins moving around; faster in phospholipids than in membrane proteins.
- Flip flopping (movement on one layer of the phospholipid will FLIP onto the other layer) is rare but does happen; only occurs when there is a charge that allows for movement between the hydrophobic tails of the phospholipid bilayer. Catalyzed by phospholipid translocase (aka “flip-flop”-ase)
What are factors that affect fluidity?
- Presence of double bonds, specifically cis (creates kinks)
- Length of the fatty acid (short = more fluid bc less contact room for reactions)
- Presence of Sterols: hydrophobic; used for membrane structure (in animals) and hormones; allows for more fluidity at low temperatures by “pushing” apart the packing of phospholipids, and less at high by reducing phospholipid bilayer movement → Cholesterol (animals), sitosterol (plants), ergosterol (fungi)
- Cellular control: ability to change lipid composition when temperatures vary in order to maintain stable fluidity
Membrane Proteins + 2 Types, defined
Functions: passage across membrane; receptor; enzyme; adhesion; cell communication; energy transformation
Bi-facial, therefore can vary in lipids, proteins, carbohydrates, fluidity → therefore, composition will vary.
- Integral proteins: strong transmembrane association, therefore can operate on both sides; either anchored in hydrophobic regions of the bilayer
- - Alpha helices: transmembrane; can be single spanning (pass through the membrane once) or multiple spanning (multiple passings; usually common for proteins to be 6 or 7)
- - Unilaterals: strong association by being covalently bonded to a phospholipid / glycolipid / etc on ONE SIDE of the membrane - Peripheral proteins: weak interactions with integral protein / phospholipid / pr carbohydrate therefore only exists on ONE SIDE of the membrane
Movement of membranes via vesicles:
- Principle of topological equivalence
- factors that affect permeability
Principle of topological equivalence: The side of the membrane facing the cytosol has always faced the cytosol.
What are factors that affect permeability?
Size of molecule
Polarity
Charge
Consider: Nonpolar molecules (lipid soluble) and small polar uncharged (water, glycerol) can cross the membrane BUT Large polar uncharged (glucose, sucrose) molecules and ions (Na+, Mg++, Cl-) cannot cross.
Types of Membrane Movement (3)
- Simple diffusion: passive transport (no energy cost) powered by concentration gradient; for small polar molecules are lipid soluble molecules
- Facilitated diffusion: involve transport proteins (channel and carrier) for ions and large polar molecules
- - Osmosis: movement of water across a membrane from a area of low [solute] to an area of high [solute] bc high [solute] indicates low [water]
- - channel proteins: gated hydrophilic tunnel, like aquaporins which allow massive amounts of water transport
- - carrier proteins (permease): physically carry across membrane using conformational changes; Specific for solute transported because the binding site is specific; can be saturated or inhibited by a similar molecule or dissimilar molecule that alters its conformation - Active transport: can move material against the concentration gradient WITH AN ENERGY COST; involves only carrier proteins
- - ATP driven pumps: phosphate group donated by ATP creates a conformational change; can dephosphorylate to return to original shape; creates a concentration gradient for [solute 1]
- - Co transport: combines features of facilitated diffusion and ATP pumps to allow downhill diffusion of [solute 1] through the carrier protein WHILE ALSO CARRYING [solute 2] AGAINST its concentration gradient → symporter: carry solutes in same direction (H+ / sucrose) VERSUS antiporter: carry solutes in different directions (Na/K pump)
Basal and Apical Sides of an Epithelial Cell (ie. glucose from the small intestine)
- defined
- pathway
APICAL: aka the business side; faces towards the lumen of the small intestine; location of NA+ / Glucose co transporter (can also have GLUT-2 but v rare)
BASAL: faces away from the lumen and towards the blood; location of facilitated carrier (specifically GLUT-2 that can transport glucose into the blood) and NA+ / K+ ATPase
PATHWAY:
- NA+/K+ ATPase: pays ATP to pump 3 NA+ out and 2 K+ in, creating a higher [NA+] outside the cell and a higher [K+] inside the cell → stroma is “positive” and the lumen is “negative”
- NA+ / Glucose cotransporter: symporter; takes both into the cell bc [glucose] is lower outside than inside and thus is moving AGAINST its gradient
- GLUT-2: facilitated transport of glucose from cell into the blood; high to low concentration
- IF [GLUCOSE] IS LOW INSIDE AND HIGH OUTSIDE: the Na+ / Glucose co-transporter shuts down due to the favorable gradient of glucose into the cell and GLUT-2 can be inserted into the apical side and allow for facilitated diffusion
Define the following:
- Bulk flow
- Chemical signalling
BULK FLOW: refers to the movement of large polar molecules
- Requires energy and movement along the cytoskeleton
- Endocytosis: movement into the cell → ie. phagocytosis
- Exocytosis: movement out of the cell → ie. transport vesicle fuses with plasma membrane
CHEMICAL SIGNALLING:
- Respond to surroundings or other cells
- Multicellularity: coordination of local activities, homeostatic responses within the tissues and organs)
- Signaling cell secretes a chemical signal (aka ligand; binds to a site on a target cell); remains OUTSIDE the cell membrane
- Target cell: equipped with a receptor (usually a protein) to accept the ligand, triggering a change in behavior of the cell