Biochem Stuff
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| function of Edman degradation | sequence of amino acids (primary structure)
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| function of peptide bond hydrolysis | determining amino acid composition of protein
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| function of X-ray crystallography | determining secondary/tertiary/quaternary structure
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| ion exchange chromatography separates based on... | charge
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| reverse phase/hydrophobic chromatography separates based on... | hydrophobicity
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| affinity chromatography separates based on... | affinity for certain ligand
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| gel filtration separates based on.../(prepatory or analytical?) | size/molecular weight, PREPARATORY
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| SDS-PAGE chromatography separates based on.../(prepatory or analytical?) | relative size, BEST WAY for determining molecular weight, ANALYTICAL
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| forces that stabilize 3D structure (5) | electrostatic, H-bonding, Van der Waals forces, hydrophobic interactions, disulfide bonds (and salt bridges)
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| 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
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| ligands that can be attached to affinity chromatography resin | substrates, coenzymes, metal ions, nucleotides, antibodies
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| possible causes of HYPERproteinemia (2) | disease/damage to liver (hepatitis, cirrhosis), severe dehydration leading to hemoconcentration
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| possible causes of HYPOproteinemia (3) | water intoxication (excessive water --> hemodilution), kidney malfunction, fluid loss in severe burn patients
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| globular proteins consist mainly of AAs with ____ sidechains | small, short
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| fibrous proteins consist mainly of AAs with ____ sidechains | long
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| most abundant protein in blood | albumin
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| enzymes can be controlled by... (4) | allosteric control, covalent modification (phosphorylation), proteolytic activation (zymogens), availabilty of enzyme
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| physical instabilities of proteins | denaturation (loss of folding structure)--> change in pH, temp, ionic strength, other solute concentrations
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| The Michaelis-Menton Equation! | V0 = Vmax * [S] / Km + [S]
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| LB plot (x-intercept) | -(1/Km)
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| LB plot (slope) | (Km/Vmax)
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| LB plot (y-intercept) | (1/Vmax)
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| Km approximates the association-dissociation of (E, S, ES, E+P)? | ES
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| when the BODY uses enzyme inhibition, it uses ______ inhibition | allosteric
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| when pharmaceuticals inhibit enzymes, they (usually) use _______ inhibition | competitive
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| the effects of COMPETITIVE inhibition on: Km, Vmax, slope of LB line | Km INCREASES (LESS affinity)
Vmax CONSTANT
slope INCREASES
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| the effects of "NONCOMPETITIVE" inhibition on: Km, Vmax, slope of LB line | Km CONSTANT
Vmax DECREASES
slope INCREASES
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| the effects of "UNCOMPETITIVE" inhibition on: Km, Vmax, slope of LB line | Km INCREASES
Vmax DECREASES
slope ????
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| What is the major difference between coenzymes and prosthetic groups? | coenzymes are NOT COVALENTLY ATTACHED, while prosthetic groups ARE COVALENTLY ATTACHED!
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| populations at risk for vitamin deficiencies (6) | children, pregnant women, older adults, teenagers+20-somethings on low-calorie diets, smokers, and alcoholics
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| catabolism involves | BREAKDOWN
OXIDATION of fuels
OXIDATIVE power
REDUCED coenzymes (result)
NAD+/NADH and FAD+/FADH2
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| anabolism involves | BUILD UP
REDUCTION of substrates
OXIDIZED coenzymes (result)
NADP+/NADPH
REQUIRES ENERGY!
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| the most abundant protein in bones, tendons, cartilage, and skin | collagen
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| 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
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Created by:
ianray42
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