Amino Acids, Peptides, and Proteins Flashcards

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1
Q

All chiral amino acids used in eukaryotes are…

A

L-amino acids, which means NH3 is on the left side of Fisher Projection

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2
Q

Exception to (S) absolute configuration

A

cysteine (R group has higher priority)

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3
Q

Nonpolar and nonromantic

A
glycine
alanine
leucine
valine
isoleucine 
methionine 
proline
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4
Q

Aromatic side chain

A

tryptophan
tyrosine
phenylalanine

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5
Q

Polar side chains

A
serine
threonine 
asparagine
glutamine
cysteine
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6
Q

Acidic side chains

A

Glutamate and Aspartate (negatively charged at physiological pH)

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7
Q

Basic side chains

A

Lysine
arginine
histidine

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8
Q

Type of ring on histidine

A

imidazole –> aromatic ring with two nitrogens

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9
Q

If pH is < pKa

A

protonated form predominates

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10
Q

pKa for COOH

A

around 2

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11
Q

pKa doe NH2

A

around 9

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12
Q

isoelectric point

A

pH at which the molecule is electrically neutral

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13
Q

pI neutral amino acid

A

pKa NH + pKa COOH / 2

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14
Q

pI acidic amino acid

A

pKa R group + pKa COOH / 2

R group is COOH (acidic)

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15
Q

peptide bonds

A

condensation, dehydration, acyl substitution reaction

partial double bond character

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16
Q

chymotrypsin

A

cleaves COOH end of Phe, Trp, Tyr

17
Q

trypsin

A

cleaves COOH end of Lys, Arg

18
Q

general way in which enzymes break peptide bonds:

A

add H to the amino group and OH to carbonyl carbon

19
Q

alpha helices

A

rodlike structure in which chain coils clockwise.
stabilized by H-bonds between carbonyl O and amide H
R groups point away from core

20
Q

proline in secondary structures

A

found in the turns of beta-sheets and as the residue at the start of alpha helix

21
Q

disulfide bonds

A

important in tertiary structures

forms between cysteine molecules that become oxidized to form cystine

22
Q

conjugated protein

A

derive part of their function from covalently attached molecules called prosthetic groups (vitamins, metal ions,)

23
Q

what can cause protein denaturation?

A

temperature
urea
detergents (SDS)