Basic Chemical Context of Life notes Flashcards
organisms are made up of ____
matter
matter
anything that takes up space and mass
electronegativity
ability of an atom to attract electrons
EN between two atoms directly affects what type of bond it forms
Ionic bond
the complete transfer of electrons from one atom to another
more electronegative atom pulls an electron from the less electronegative atom
results in a difference in charge between the atoms
covalent bond
sharing of electrons between atoms with similar electronegativities
single, double, or triple
nonpolar covalent bond
equal sharing of electrons
no atom has a greater pull of electrons than the other - identical electronegativities
polar covalent bond
unequal sharing of electrons
leads to formation of a dipole
hydrogen bond
a weak bond that can form between molecules that have a hydrogen atom attached to a highly electronegative atom (F, O, or N) that is attracted to a negative charge on another atom
- can be within a molecule (intramolecular) or between molecules (intermolecular)
- important bond in water and DNA
Van der Waals interactions
are a weak attraction rather than a true chemical bond
due to different distribution of electrons
- weaker and more transient than hydrogen bonds
- interaction gets stronger the larger the molecule is
- happens as electrons orbit the atom and there is a change is distribution
water
- polar molecule
- excellent solvent - the dipoles of H2O break up polar or charged ionic molecules
- high heat capacity - a lot of heat has to be added before the temperature changes (good thing! means water is temperature stable)
- more dense as a liquid than a solid
- ice floats - water expands as it freezes and becomes less dense than liquid form
- cohesion/surface tension - water is attracted to like substances due to its H bonds. this strong cohesion between water molecules produces a high surface tension
- adhesion - water is also attracted to unlike substances
Hydroxyl (OH)
polar and hydrophilic
carboxyl (COOH)
polar, hydrophilic, weak acid
amino (NH2)
polar, hydrophilic, weak base
phosphate
polar, hydrophilic, acid
carbonyl
- aldehyde
- ketone
polar and hydrophilic
methyl (CH3)
nonpolar and hydrophobic
monosaccharide
singular sugar molecule
(glucose or fructose)
alpha - OH down
beta - OH up
disaccharide
two sugar molecules joined by glycosidic linkage
(sucrose, lactose, maltose)
polysaccharide
series of connected monosaccharides; polymer
(glucose + fructose)
(glucose + galactose)
( glucose + glucose)
starch
a polymer of alpha-glucose molecules
- store energy in plant cells
glycogen
a polymer of alpha-glucose molecules
- store energy in animal cells
cellulose
a polymer of beta-glucose
- structural molecules for walls of plant cells and wood
chitin
a polymer similar to cellulose, except each beta-glucose group has a nitrogen containing group attached to the ring
- structural molecule in fungal cells as well as insect exoskeletons
lipids
hydrophobic molecules that function in insulation, energy storage, make up structural components like cholesterol and phospholipids in membranes, and participate in endocrine signaling
triglycerides
describe structures consisting of three fatty acid chains attached to a glycerol backbone. Can be saturated or unsaturated
saturated
contain no double bonds and have straight chains; are bad for health since the straight chains stack densely and form fat plaques
unsaturated
contain double bonds that cause kinks in chains; are better for health since chains stack less densely
can be cis or trans
phospholipids (diaclglycerols)
comprised of two fatty acids and a phosphate group (+R) attached to a glycerol backbone
- are amphipathic, which means has both hydrophobic and hydrophilic properties
steroids
comprised of three 6-membered rings and one 5-membered ring; include hormones and cholesterol
lipid derivatives/structures
- phospholipids
- waxes - esters of fatty acids and monohydroxylic alcohols, used as a protective coating on the skin
- steroids - sex hormones, cholesterol, corticosteroids - 4 ringed structures
-
carotenoids - fatty acid carbon chains with conjugated double bonds and five/six-membered carbon rings at each end. includes pigments which produce colors in plants and animals
* subgroups are carotenes and xanthophylls - porphyrins - 4 joined pyrrole rings that often complex with a metal (porphyrin heme complexes with fe in hemoglobin; chlorophyll with Mg)
-
adipocytes - specialized fat cells in two categories
* white fat cells - composed primarily of triglycerides with a thin layer of cytoplasm around it
* brown fat cells - have considerable cytoplasm, lipid droplets scattered throughout, and lots of mitochondria - glycolipids - similar to phospholipids but they have a carbohydrate group instead of a phosphate group
- lipoproteins - lipids are insoluble so they are transported in the blood via lipoproteins, which are lipids cores surrounded by phospholipids and apolipoproteins
cell membrane fluidity
cell membranes need to maintain a certain degree of fluidity and are capable of changing membrane fatty acid composition to do so
- in cold weather - cell membranes become more rigid. in order to avoid rigidity, cholesterol and mono and polyunsaturated fatty acids are incorporated into the membrane, which increases fluidity
- in warm weather - cell membranes become more fluid and flexible. in order to avoid cell membrane collapse, cholesterol is added to restrict movement. the fatty acid tails are saturated so they become straight and pack tightly, thus decreasing fluidity
amino acid structure
amino group
carbon side chain
carboxyl group
proteins
polymers of amino acids joined by peptide bonds.
protein functions
- storage proteins - casein in milk, ovalbumin in egg whites, and zein in corn seeds
- transport proteins - hemoglobin carries oxygen, cytochromes carry electrons
-
enzymes - catalyze reactions in both forward and reverse directions
* efficiency is determined by substrate and enzyme concentration, temperature, pH and presence/absence of any inhibitors
* amylase catalyzes reactions that break alpha-glycosidic bonds in starch -
cofactors - non-protein molecules that assist enzymes; the union of a cofactor + enzyme is a holoenzyme (when an enzyme is not combined with a cofactor, it is called and apoenzyme/apoprotein)
* if the cofactor is organic, it is a coenzyme
* if a cofactor is covalently bound to an enzyme, it is called a prosthetic group
protein classification
-
simple - formed entirely of amino acids
- albumins & globulins - functional proteins that act as carriers or enzymes
- scleroprotein - fibrous proteins, have structural function (e.g. collagen) -
conjugated - simple protein + non-protein
- lipoprotein - protein bound to lipid
- mucoprotein - protein bound to carbohydrate
- chromoprotein - protein bound to pigmented molecule
- metalloprotein - protein complexed around metal ion
- nucleoprotein - contains histone or protamine, bound to nucleic acid
primary protein structure
sequence of amino acids connected by peptide bonds
secondary protein structure
3D shape resulting from hydrogen bonding between amino acid and carboxyl groups of adjacent amino acids (alpha helix or beta sheet)
tertiary protein structure
3D structure that forms primarily due to non-covalent interactions between amino acid R groups
- non-covalent interactions include H-bonds, ionic bonds, hydrophobic effect (R groups push away from water), and Van der Waals forces
- includes disulfide bonds (strong type od covalent bond between cysteins) which contribute to tertiary structure
quaternary protein structure
3D shape of a protein that is a grouping of two or more separate peptide chains
globular proteins
- somewhat water soluble
- mostly tertiary
- diverse functions: enzymatic, hormonal, inter and intracellular storage, transport, osmotic regulation, immune response
fibrous/structural proteins
- not water soluble
- mostly secondary
- made of long polymers
- function: maintain and add strength to cellular and matrix structure (collagen or keratin)
membrane proteins
includes proteins that function as membrane pumps, channels, or receptors
protein denaturation
when proteins are taken out of their ideal temperature, pH range, or solvent, denaturation can occur
means the protein is reversed back to its primary structure
nucleic acids
overall term for DNA and RNA, essential to all forms of life
function: to encode, express, and store genetic information
nucleotides
monomers that make up nucleic acids and consist of a nitrogenous base, 5C sugar, and a phosphate group
Cell Theory
states that
- all living organisms are comprised of one or more cells
- the cell is the basic unit of structure, function, and organization in all organisms
- all cells come from preexisting, living cells
- cells carry hereditary information
RNA World Hypothesis
proposes that self-replicating RNA molecules were precursors to current life. also states that RNA stores genetic information like DNA and catalyzes chemical reactions, leads to the belief that RNA may have played a major role in evolution
central dogma of genetics
states that biological information cannot be transferred backwards from protein to protein or nucleic acid. Rather, information must travel from:
DNA –> RNA –> proteins
stereomicroscope
uses visible light to view the surface of a sample
pro: can view living samples
con: has low light resolution compared to a compound microscope
compound microscope
uses visible light to view a thin section of a sample
pro: can view some living samples (single cell layer)
con: may require staining
phase contrast microscope
uses light phases and contrast for a detailed observation of living organisms, including internal structures if thin
pro: has good resolution and contrast
con: not ideal for thick samples and produces a “halo effect” around perimeter samples
confocal laser scanning microscope and fluorescence
used to observe thin slices while keeping a sample in tact; common method for viewing chromosomes during mitosis
pro: can observe specific parts of cell using fluorescent tagging
con: can cause artifacts
can be used without fluorescence, dye specimen
scanning electron microscope (SEM)
pro: view surface of 3D objects with high resolution
con: can’t use on living samples, preparation is extensive as sample needs to be dried and coated; costly
cyro SEM
similar to SEM
pro: sample is not dehydrated so you can observe samples in their more ‘natural form’
con: can’t use on living samples, samples must be frozen, which can cause artifacts
transmission electron microscope (TEM)
pros: can observe very thin cross-sections in high detail, and can observe internal structures with very high resolution
cons: cannot be used on living samples, preparation of sample is expensive, and technique is costly
electron tomography
not a type of microscope, but a technique used to build up a 3D model of sample using TEM data
pro: can look at objects in 3D and see objects relative to one another
con: same as TEM, cannot be used on living samples, costly
centrifugation
common technique used to prepare a sample for observation or further experimentation. it spins and separates liquified cell homogenates into layers based on density
for cell based on highest density to lowest:
nuclei layer -> mitochondria/chloroplasts/lysosome -> microsomes/small vesicles -> ribosomes/viruses/larger macromolecules
differential centrifugation
forms continuous layers of sediment, where insoluble proteins are found in the pellet while soluble proteins remain in the supernatant, liquid above the pellet
enzyme functions
recall that enzymes are globular proteins that act as catalysts
role of ATP
ATP is a common source of activation energy, and the compound stores its potential energy in the form of chemical energy. new ATP is formed via phosphorylation, ADP and phosphate come together using energy from an energy rich molecule like glucose
regulation of enzymes
enzymes must be strictly regulated to ensure that they are only functional for specific use
Km
Michaelis constant, and represents the substrate concentration at which the rate of reaction is half of the max velocity of the enzyme, or Vmax
- a small Km indicates that an enzyme requires only a small amount of substrate to reach max velocity
- a higher Km means the enzyme needs more substrate to reach max velocity
allosteric enzymes
have both an active site for substrate binding and an allosteric site for the binding of an allosteric effector (can be an activator or inhibitor)
competitive inhibition
a substance that mimics the substrate and inhibits the enzyme by binding at the active site. the effect of competitive inhibition can be overcome by increasing substrate competition
Km raised but Vmax is not