Exam 1 Flashcards
hydrophobic effect
increases entropy by freeing water molecules
number of unordered water molecules increases
peptide bond formation
dehydration/condensation, water removed
peptide bond breaking
hydrolysis, water is added
omega bond can either be ___ or ____ and is usually
180, 0, 180
which bond can rotate freely
phi and psi
phi
n - ca
psi
ca-c
which aa has more areas on rp
glycine
which aa has less areas on rp
proline
pka is what for protons
when pka=ph, 50% of protons are lost
what is the best buffering for a weak acid
+/- 1 ph from the pka
pka 1 for amino acids with neutral side chains
2
pka2 for amino acids with neutral side chains
9
if given a peptide with lots of rkh, what does this mean about pi
high pi
is pi is 2,3,4 what does this mean abt side chains
acidic side chains present
pi is the point where
the net charge on the protein is 0
at a pH below the pi
more protons available, side chains protonated, will have + charge
at pH above the pI
protons LEAVE, side chains are DEPROTONATED, there will be - charge
lower pI =
more acidic side chains (ED), easily deprotonated at physiological pH
higher pI
more basic side chains (RKH), harder to deprotonate at physiological pH
primary protein structure
linear arrangement of amino acids from n to c
secondary protein structure
regularly repearting pattern of H bonding from backbone chain
tertiary protein structure
many interactions between side chain to form 3d shape
quant protein structure
multiple tertiary structures associate w each other