unit 1 exam Flashcards
what is the hydrophobic effect
the favorable increase in entropy of water when it is released from nonpolar molecules
characteristics of peptide bonds
partial double bond character between carbonyl carbon and amide nitrogen
specific activity formula
activity/total protein (units/mg)
number of H-bonds in alpha helix
(# amino acids)-4
uses for gel electrophoresis
separate molecules by size; unfold protein but maintain primary structure
does lower Kd correspond to ligand binding more or less tightly
more tightly
myoglobin properties
oxygen storage protein
binds to heme (porphyrin ring and iron atom)
iron atom in +2 ox state
monomer
bad transporter
tertiary
hyperbolic O2 binding curve
hemoglobin properties
oxygen transporter
tetramer
T state: binds less strongly to O2
R state: binds most strongly to O2
more BPG
more T state
less BPG
more R state
high affinity state conditions
more R state, less BPG, higher pH, less O2 released
(fetal hemoglobin has less BPG)
low affinity state conditions
more T state, more BPG, lower pH, more O2 released
Michaelis-Menten assumptions
k-2 is negligible
[ES] is constant
oxyanion hole purpose (chymotrypsin)
stabilizes transition state (2x in peptide breaking)
hydrophobic pocket purpose (chymotrypsin)
substrate binding specificity
histidine purpose (chymotrypsin)
gen acid/base
take H+ from ser, protonate amide, take H from H2O, protonate ser