exam 1

N-C(alpha) bond angle, limited bc it brings sidechains too close together

V=(Kcat[E][s])/(Km+[s])

inactive form of enzyme

every 3rd to 4th is on the same side, gives hydrophobic effect

C-C(alpha) bond angle, limited bc it brings sidechains too close together

H-bonding, Steric strain

parralel- N terminus and c terminus line up. Antiparallel- N and c terminus alternate

alpha helix and beta sheet

loops, hairpins, anything other than alpha helix or beta sheet

water soluble, compact and highly folded

stiff elongated conformation, forms fibers

micelle=cirlce of amphipaths, bilayer=2 sheets, vesicle= cone

pH=-log(|H+|)

Ka, pKa

pH=pKa+log(A-/HA)

where a buffer can successfully neutralize pH, flat part of curve

H+ + HCO3(bicarbonate)->H2CO3->H2O + CO2

excretes acid to reclaim bicarbonate, forms new bicarb through CO2 metabolism

phosphate on 5' position

phosphate in 3' position

deoxy, sugar on 3'

can cause mis-bonding

vanderwals, h-bonds, hydrophobic effect, ionic interactions

GC rich strands harder to denature do to stacking(not H bonding),

supercoiling

hydrolyze amino acids

hydrolyze phosphodiester bond on the outsides of the strand

hydrolyze phosphodiester bond within the strand, recognize palindromes, sticky vs blunt ends

alternate side and whether or not facing page

fairly rigid, some double bond character

no stablization from outward facing sidechain

not H bond donor

one side is more polar, other side is not

recognizable combos of secondary structure, helix bundle, helix-loop-helix, hairping, beta-sandwhich

zinc binds to DNA, motif

acetylation, glycosylation(carbonate), phosphorylation

Ion exchange, Affinity, size exclusion

buffergradient, sorts by isoelectric point

noncovalent structure, oxygen storage, hydrophobic pocket (fits heme into it), pocket fits Fe2+; binds to O2

treated as dimer of alpha-beta subunits, deoxy R state, Oxy T state, naturally lies towards T state,

allosteric;2,3-BPG binds to T and locks in place, without Hb O2 affinity is too high

lower pH=greater release of O2, H+ negative allosteric effector, shifts curve to right

globular monomer, binds atp, hydrolyzes atp when in filament F-actin

ATP hydrolysis make polymerization favorable, grows faster at + end. Function:cell shape change and movement

globular protein subunits, GTP binding, direcitonal growth,

coiled coil, non-polar AA at 1 and 4 position bind coil together, hard has more sulfur, soft has less due to high Cys residues and disulfide bonds

triple helix, left handed turn, gly packs in middle bc sterics, backbone H bonding, gives strength to connective tissues(cartilage)

motor protein, ATP binding in head, crawls on actin, non processive

motor protein, processive, atp driven, carrys vesicles

redox reactions, dehydrogenases, oxidases, peroxidases, etc

2 substrates, moves one group between substrates, transferase etc

transferase for phosphate group

hydrolysis, phosphotase, nuclease, protease, peptidase. can hydrolyze carbox. acid derivatives, phosphate derivatives and anhydrides

not redox or hydrolysis, elimination of a group to give a double bond, or addition to a double bond, hydratase, decarboxylase

rearangement without loss or add. of atoms, racemase, isomerase, mutase

bond formation, atp hydrolysis, synthetase

y=O2^n/(K^n+pO2^n)

2.8 torr