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