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75 Cards in this Set

  • Front
  • Back

coenzymes

organic compounds essential to many enzyme-catalyzed reactions

proteasomes

degrade proteins no longer needed by the cell

oligomers

shorter polymers

proteome

sum of all proteins in a given cell

amphipathic

contain regions that are polar (hydrophilic) and regions that are nonpolar (hydrophobic)

osmolarity

osm = i*c = # of solutes*molarity

isotonic

equal concentation on each side of a membrane

hypertonic

higher concentration on the outside water moves out

hypotonic

higher concentration on the inside - water moves in

zwitterion

dipolar ion which can act as either an acid or a base

prosthetic group

non-amino acid part of a conjugated protein, organic or inorganic

chymotrypsin

digestive enzyme, cleaves carboxyl side of tyrosine, tryptophan, and phenylalanine

trypsin

protease, cleaves carboxyl side of lysine or arginine except when followed by proline

carboxypeptidase

cleaves peptide bond at carboxy-terminal end of peptide

van't hoff factor

i, extent of a solute's dissociation into particles

osmotic pressure

RT(ic1 + ic2 + ...)

henderson-hasselbalch

pH = pKa + log([A-]/[HA])

Beer-Lambert Law

log(I0/I) = EcI = A (absorbance)

specific activity

units/mg

dialysis

separation of particles in a liquid based on their ability to pass through a membrane

de-salting

separating soluble macromolecules from smaller molecules

differential centrifugation

separates membrane-associated material (pellet) from supernatant

isopycnic (sucrose-density) centrifugation

separates particles into layers based on their density

cation exchange chromatography

binds cations, resin is negative, mono S

anion exchange chromatography

binds anions, resin is positive, DEAE A50

molecular sieve/size-exclusion chromatography

resin w/small holes to slow down small particles

affinity chromatography

add ligand, add proteins, protein of interest binds to ligand, wash away unwanted proteins, protein of interest eluted by ligand solution

native PAGE (polyacrylamide gel electrophoresis)

mobility depends on charge and size, protein kept intact, run at extreme (usually high) pH

SDS PAGE

protein must be denatured and coated w/negative charge, size proportional to charge

DTT and βME

reduce disulfide bonds, separate peptides

isoelectric focusing

gel pH gradient, proteins stop at their pI

2D electrophoresis

isoelectric focusing and then SDS PAGE, 2D map of proteins

mass spectrometry

measures mass to charge ratio

FDNB and dansyl chloride

identifies amino terminus

Edman degradation (PITC)

amino termini labeled, cleaved, and identified; repeat to sequence entire peptide

ϕ (phi)

N - alpha C

ψ (psi)

alpha C - C

Ramachandran plots

helps visualize phi and psi angles and see possible conformations

α-keratin

2 α-helices, many disulfide bridges (hair, nails)

collagen

left handed α-chains, 3 res/turn, triple coil (tendons, cartilage)

silk fibroin

anitiparallel β-sheets, rich in ala, gly (chrysalis, spiderwebs)

domain

section of protein w/its own structure or function (active sites)

amyloid

misfolded protein structures that can form insoluble fibrils and lead to disease

amyloidosis

buildup of amyloid

prions

infections protein misfolding

θ

= [PL]/{[PL]+P} = [L]/{[L]+kd}, fraction of P sites w/ligand, protein with ligand bound/total protein

kd

1/ka, dissociation constant, where θ = 0.5

myoglobin

storage, high affinity

hemoglobin

transport, myoglobin-like subunits, T (binding) and R (not binding) states

salt bridge

bonds between oppositely charged residues

Bohr effect

more oxygen dropped off as pH decreases

BPG altitude effect

as altitude drops, oxygen levels drop and BPG rises = more drop off

immunoglobulins

bind antigens

Fab

antigen binding domain, transposable elements (variable)

Fc

crystallizable tail (constant)

t-tubules

deep invaginations of the muscle membrane so all parts can be signaled

transverse tubules

clefts lined with Ca channels in muscle fibers which allow quick Ca release throughout sarcomere

holoenzyme

intact enzyme with prosthetic group

apoenzyme

intact enzyme without prosthetic group

cofactor

small non-protein required by enzyme

Michaelis-Menten

1/V0 = Km/Vmax[S] + 1/Vmax

Michaelis constant, km

how well the enzyme binds the substrate

Vmax

how quickly the enzyme turns substrate into product

protease digestion

breaking up proteins with specific proteases one at a time and put pieces back together to sequence

tropomyosin

blocks actin fibers

troponin C

binds to Ca, moves tropomyosin away from actin filaments releasing inhibition

troponin T

links to tropomyosin

troponin I

inhibits myosin-actin connection

turnover number

kcat

competitive inhibitor

dilutes S, binds at active site, Vmax same, Km increases

uncompetitive inhibitor

binds at other site when substrate is bound and prevents from turning into product, Vmax and Km decrease

mixed inhibitor

binds to other side whether or not substrate is bound, Vmax decreases, Km increases (usually)

noncompetitive inhibitor

mixed inhibitor when Km stays the same

racemase

enzyme that changes stereochemistry, pull protein off alpha carbon and adds back to other side

transpeptidase

enzyme required for production of bacterial cell walls