MCAT A.A.
Alanine
Ala, A
Arginine
Arg, R, 12.50
Asparagine
Asn, N
Aspartate
Asp, D, 3.90
Cysteine
Cys, C, 8.40
Line-Weaver Burke Plot
EVERYTHING IS OPPOSITE
Glutamine
Gln, Q
Glutamate
Glu, E, 4.10
Glycine
Gly. G
Histidine
His, H, 6.00
Isoleucine
Ile, I
essential a.a.
KHTVWILFM
Leucine
Leu, L
Lysine
Lys, K, 10.50
Methionine
Met, M
Phenylalanine
Phe, F
Proline
Pro, P
Serine
Ser, S, 13.00
Threonine
Thr, T, 13.00
Tryptophan
Trp, W
Tyrosine
Tyr, Y, 10.50
Valine
Val, V
primary structure
a.a. sequence
nonpolar a.a.
alkyl groups; G, A, V, L, I, F, W
acidic a.a
and "evan died"- glutamic and aspartic acid; anion
pI
average two pH around 0 charge
Noncompetitive inhibition
binds at allosteric site; diminished Vmax, unchanged KM
Uncompetitive inhibitor
binds to allosteric site but only to enzyme-substrate complex; decreased Vmax and Km
basic a.a
but "he ran lousy"- histidine, arginine, lysine; cation
prosthetic group
cofactor or coenzyme that is covalently bonded to a protein to permit its function; AFTER TRANSLATION
secondary structure
hydrogen bonding between backbone groups; alpha helix, beta pleated sheets (antiparallel, parallel)
polar a.a.
hydrogen bonding; S, T, Y, N, Q
tertiary structure
interactions between side chains; hydrophobic on interior, hydrophilic on exterior
pH of a.a.
pH=pKa+log [A-] aka base form/[HA] aka acid form
V max
reaction rate at enzyme saturation
quarternary structure
same types of interactions as tertiary but between subunits
Competitive inhibition
substrate can outcompete; Km increased, Vmax unchanged
Km
substrate concentration that produces half Vmax; low Km= high affinity