Question | Answer |
function of Edman degradation | sequence of amino acids (primary structure) |
function of peptide bond hydrolysis | determining amino acid composition of protein |
function of X-ray crystallography | determining secondary/tertiary/quaternary structure |
ion exchange chromatography separates based on... | charge |
reverse phase/hydrophobic chromatography separates based on... | hydrophobicity |
affinity chromatography separates based on... | affinity for certain ligand |
gel filtration separates based on.../(prepatory or analytical?) | size/molecular weight, PREPARATORY |
SDS-PAGE chromatography separates based on.../(prepatory or analytical?) | relative size, BEST WAY for determining molecular weight, ANALYTICAL |
forces that stabilize 3D structure (5) | electrostatic, H-bonding, Van der Waals forces, hydrophobic interactions, disulfide bonds (and salt bridges) |
chemical instabilities of proteins (5) | peptide bond hydrolysis, hydrolysis of amide sidechains (glutamine/asparagine), oxidation of sulfur-containing sidechains or conjugated sidechains, reduction of disulfide bonds, racemization of L-->D amino acids |
ligands that can be attached to affinity chromatography resin | substrates, coenzymes, metal ions, nucleotides, antibodies |
possible causes of HYPERproteinemia (2) | disease/damage to liver (hepatitis, cirrhosis), severe dehydration leading to hemoconcentration |
possible causes of HYPOproteinemia (3) | water intoxication (excessive water --> hemodilution), kidney malfunction, fluid loss in severe burn patients |
globular proteins consist mainly of AAs with ____ sidechains | small, short |
fibrous proteins consist mainly of AAs with ____ sidechains | long |
most abundant protein in blood | albumin |
enzymes can be controlled by... (4) | allosteric control, covalent modification (phosphorylation), proteolytic activation (zymogens), availabilty of enzyme |
physical instabilities of proteins | denaturation (loss of folding structure)--> change in pH, temp, ionic strength, other solute concentrations |
The Michaelis-Menton Equation! | V0 = Vmax * [S] / Km + [S] |
LB plot (x-intercept) | -(1/Km) |
LB plot (slope) | (Km/Vmax) |
LB plot (y-intercept) | (1/Vmax) |
Km approximates the association-dissociation of (E, S, ES, E+P)? | ES |
when the BODY uses enzyme inhibition, it uses ______ inhibition | allosteric |
when pharmaceuticals inhibit enzymes, they (usually) use _______ inhibition | competitive |
the effects of COMPETITIVE inhibition on: Km, Vmax, slope of LB line | Km INCREASES (LESS affinity)
Vmax CONSTANT
slope INCREASES |
the effects of "NONCOMPETITIVE" inhibition on: Km, Vmax, slope of LB line | Km CONSTANT
Vmax DECREASES
slope INCREASES |
the effects of "UNCOMPETITIVE" inhibition on: Km, Vmax, slope of LB line | Km INCREASES
Vmax DECREASES
slope ???? |
What is the major difference between coenzymes and prosthetic groups? | coenzymes are NOT COVALENTLY ATTACHED, while prosthetic groups ARE COVALENTLY ATTACHED! |
populations at risk for vitamin deficiencies (6) | children, pregnant women, older adults, teenagers+20-somethings on low-calorie diets, smokers, and alcoholics |
catabolism involves | BREAKDOWN
OXIDATION of fuels
OXIDATIVE power
REDUCED coenzymes (result)
NAD+/NADH and FAD+/FADH2 |
anabolism involves | BUILD UP
REDUCTION of substrates
OXIDIZED coenzymes (result)
NADP+/NADPH
REQUIRES ENERGY! |
the most abundant protein in bones, tendons, cartilage, and skin | collagen |
biochemical pathways are regulated by... (4) | -covalent modification (e.g. phosphorylation)
-compartmentation into different cell locations
-isolation to specific organs
-synthesis and degradation of pathway enzymes |