Question Answer
Alanine A
Cysteine C
aspartic acid D
phenylalanine F
glycine G
histidine H
isoleucine I
Lysine K
Leucine L
Methionine M
Asparagine N
Proline P
Glutamine Q
Arginine R
Serine S
Threonine T
Valine V
Tryptophan W
Tyrosine Y
Glutamine Z
Hydrophobic Amino Acids glycine (G), alanine (A), proline (P), valine (V), leucine (L), isoleucine (I), phenylalanine (F), tyrosine (Y), tryptophan (W), methionine (M)

GAPVLIFYWM

Branched chain Amino Acids valine (V), leucine (L), isoleucine (I)

VLI

non polar & hydrophobic amino acids glycine (G), alanine (A), proline (P), valine (V), leucine (L), isoleucine (I), phenylalanine (F), methionine (M)
polar, uncharged amino acids serine (S), threonine (T), tyrosine (Y), tryptophan (W), asparagine (N), glutamine (Q)

STYWNQ

polar, uncharged OH groups and phosphorylate serine (S), threonine (T), tyrosine (Y)

STY

n-side chain glycosylation
negatively charged amino acids aspartate (D), glutamate (E)

DE

backbone of Amino acids alpha carbon + amino group + carbonyl group
positively charged basic molecules: arginine (R), lysine (K), histidine (H)

RKH

3 protein families globular, fibrous, membrane spanning
in hemoglobin, iron can be ferric (3+) or ferrous (2+)
heme binds oxygent ferrous (2+)
primary hemoglobin in adults HbA
fetal hemoglobin binds more readily to carbon monoxide
if delta G is positive, amino acids remain in hydrophobic side
if delta G is negative, amino acids migrate into aqueous solution
What is the H+ concentration in a urine sample that has pH of 6 10^-6M
weak acids are incompletely dissociated in solution
how many equivalents of base need to be added to an acid soution for the PH to equal the pKa 0.5
what is the best buffering range of the monoprotic acid MOPS, pka = 7.2 pH 6.5-8.5
due to the side group steric clash, almost all peptide bonds are trans
which residues are most likely found in turns? R, G, D
which residues are most likely to be found in DNA binding helixes? K,R,Q
which residues are most likely to be found on the inside surface of a porin? K,S,Q
Which amino acid is redox active? C
which residues are most likely to be found on the inside surface of a protein? M,L,F
changes in what level of structure are responsible for creating amyloid fibers? secondary
what is a critical feature of the Michaelis-menten model of enzyme catalysis? formation of an ES complex
at pH=8 mutation of histidine to which amino acid would be conservative? N
In competitive inhibition, what does the inhibitor do? it binds reversibly at the active site
in uncompetitive inhibition, what does the inhibitor do? it binds only to the ES complex
in non competitive inhibition, what does the inhibitor do? it lowers the characteristic V max of the enzyme


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