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31 Cards in this Set

  • Front
  • Back
Type of amino acids found in nature?
L-amino acids
Highly Hydrophobic AAs
Less Hydrophobic
Highly Hydrophilic
Present within one species, different functions
present within diff species, same function
primary structure forces
peptide bonds
secondary structure forces
H-bonds, van der waals
tertiary structure forces
covalent bonds (disulfide bridges), non-cov interactions(electrostatic, van der waals, hydrophobic)
quaternary structure forces
covalent bridges, non covalent interactions
proteins can be denatured by
heat, extreme changes in pH, chemicals (SDS, urea, mercaptoethanol)
ion exchange
polymer beads with charged groups
gel filtration
porous beads, smaller get stuck, larger pass through
polymer bound ligand for protein of interest
Electrophoresis - reagent? which move further, larger or smaller
SDS added. Larger move slower, since they are held up by the gel
SDS Page Axises
X right, decreasing pH
Y down, decreasing Mw
How can Cystine bridges be broken?
oxidation by performic acid
reduction by DTT, then acetylation by iodoacetate
What reagents determine the N-terminal amino acid only?
flurodinitrobenzene, dabsyl chloride, dansyl chloride
What reagent is used for edman degradation?
phenyl isothiocyanate
Where does trypsin break?
C-Lys, Arg
Where does chymotrypsin break?
Where does staph protease break?
Where does cyanogen bromide break?
enzyme units
the amount of enzyme, that, under defined conditions, will catalyze the trans of 1 umol of substrate per min
specific activity
number of enzyme units per mg
Michaelis-menton equation
V0=Vmax*[S] / Km+[S]
Michaelis constant
Lineweaver-burk equation
1/V0=Km/Vmax * 1/[S] + 1/Vmax
Effect of 2,3BPG on hemoglobin
binds in a cleft in T form, stabilizing it, reducing O2 affinity
Effect of H+ on hemoglobin
favors T state, releasing O2
Carbonic anhydrase equation
H+ + HCO3- <--> CO2 + H20