Amino Acids, Peptides, and Proteins Flashcards

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1
Q

Nonpolar, nonaromatic side chains

A

glycine, alanine, valine, leucine, and isoleucine

methionine (sulfur atom but considered relatively nonpolar)

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2
Q

Chirality of amino acids in eukaryotes ?

A

L-amino acids (S) absolute configuration;

exception: cysteine –> L amino acid (has R absolute configuration)

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3
Q

Only cyclic, nonpolar, nonaromatic

A

proline

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4
Q

Aromatic side chains?

A

tryptophan, phenylalanine, tyrosine

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5
Q

Polar side chains?

A

Serine, threonine (both have -OH groups), asparagine, glutamine (have amide side chains), cysteine (thiol, -SH)

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6
Q

negatively charged (acidic) side chain

A

aspartic acid (asparatate) and glutamic acid (glutamate)

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7
Q

positively charged (basic) side chains

A

lysine, arginine, histidine (has an aromatic ring with two nitrogen atoms/called a imidazole)

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8
Q

hydrophobic amino acids

A

alanine, isoleucine, leucine, valine, and phenylalanine

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9
Q

hydrophilic amino acids

A

charged side chains–> positively charged histidine, arginine, and lysine plus negatively charged glutamate and aspartate

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10
Q

alanine

A

ala, A

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11
Q

arginine

A

arg, R

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12
Q

asparagine

A

Asn, N

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13
Q

Aspartic acid

A

asp, D

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14
Q

Cysteine

A

cys, C

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15
Q

Glutamic acid

A

Glu, E

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16
Q

Glutamine

A

Gln, Q

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17
Q

Glycine

A

Gly, G

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18
Q

Histidine

A

His, H

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19
Q

Isoleucine

A

Ile, I

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20
Q

Leucine

A

Leu, L

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21
Q

Lysine

A

Lys, K

22
Q

Methionine

A

Met, M

23
Q

Phenylalanine

A

Phe, F

24
Q

Proline

A

Pro, P

25
Q

Serine

A

Ser, S

26
Q

Threonine

A

Thr, T

27
Q

Tryptophan

A

Trp, W

28
Q

Tyrosine

A

Tyr, Y

29
Q

Valine

A

Val, V

30
Q

amphoteric species

A

can accept a proton or donate a proton

31
Q

zwitterions

A

have a positive and negative charge

32
Q

isoelectric point

A

where the net charge is 0, pH at which the molecule is electrically neutral

33
Q

peptide bonds

A

when an amide bond is formed between the -COO- group of one amino acid and the NH3+ group of another amino acid

34
Q

What type of reaction is the formation of a peptide bond?

A

A condensation/dehydration reaction…results in the removal of a water molecule; the nucleophilic amino group of one amino acid attacks the electrophilic carbonyl group of another amino acid

35
Q

How are peptide bonds structured?

A

From N-terminus to C-terminus, free amino end on the left, carboxyl end on the right

36
Q

primary structure

A

linear arrangement of amino acids coded in an organism’s DNA, can be determined by sequencing

37
Q

secondary structure

A

local structure of neighboring amino acids, result of hydrogen bonding between nearby amino acids, most common secondary structures are alpha-helices and B-pleated sheets

38
Q

What is an important component of keratin?

A

alpha helix, keratin is a fibrous structural protein found in human skin, hair, and fingernails

39
Q

beta-pleated sheets

A

can be parallel or antiparallel, fibroin (a primary protein component of silk fibers) is composed of beta-pleated sheets, often see prolines, help turn between beta-pleated sheets

40
Q

proline’s role in secondary structure

A

helps form turns in alpha helices or beta sheets, creates a kink

41
Q

fibrous proteins

A

collagen, resembles long strands/sheets

42
Q

globular proteins

A

globin, tends to be spherical, like a globe

43
Q

tertiary structure

A

3-D shape of a protein, mostly determined by hydrophilic and hydrophobic interactions between the R groups of amino acids, have disulfide bonds

44
Q

what forms disulfide bonds?

A

two cysteine molecules become oxidized to form cystine, disulfide bonds create loops in the protein chain

45
Q

What is it called when a protein loses its tertiary structure?

A

Denaturation, it will lose its function, often irreversible

46
Q

quaternary structure

A

not all proteins have quaternary structure, need multiple subunits to have it, hemoglobin and immunoglobulins are classic examples

47
Q

prosthetic groups

A

covalently attached molecules

48
Q

What is true at the pKa

A

[HA]=[A-]

49
Q

What does the titration curve look like at the pKa values of the amino acid?

A

Nearly flat

50
Q

What does the titration curve look like at the pI of the amino acid?

A

Nearly vertical

51
Q

What type of reaction is the breaking of a peptide bond?

A

A hydrolysis reaction (water is used to break down the bonds of a particular substance)

52
Q

Hydrophobic interactions

A

push hydrophobic R groups to the interior of a protein, which increases entropy of the surrounding water molecules to create negative Gibbs free energy