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BIOC3021 > Amino Acids > Flashcards

Amino Acids Flashcards

1
Q

amino acids consist of what 4 groups connected to the central alpha carbon?

A

amino group, carboxyl group, R side chain, hydrogen bond

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2
Q

NH2 is what type of group?

A

amino

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3
Q

COOH is what type of group?

A

carboxyl

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4
Q

At physiological pH, amino group is _____ and looks like NH3+

A

protonated

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5
Q

At physiological pH, the carboxyl group is _________ and looks like COO-

A

unprotonated

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6
Q

The R side chain, amino group, hydrogen, and carboxyl group and bounded by what type of bond?

A

covalent

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7
Q

How many nonpolar/hydrophobic amino acids are there?

A

8

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8
Q

ALA, A

A

alanine

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9
Q

VAL, V

A

valine

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10
Q

LEU, L

A

leucine

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11
Q

ILE, I

A

isoleucine

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12
Q

PRO, P

A

proline

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13
Q

MET, M

A

methionine

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14
Q

PHE, F

A

phenylalanine

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15
Q

TRP, W

A

tryptophan

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16
Q

alanine is a ___ amino acid

A

nonpolar/hydrophobic

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17
Q

valine is a _____ amino acid

A

nonpolar/hydrophobic

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18
Q

leucine is a ____ amino acid

A

nonpolar/hydrophobic

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19
Q

isoleucine is a ____ amino acid

A

nonpolar/hydrophobic

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20
Q

proline is a ____ amino acid

A

nonpolar/hydrophobic

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21
Q

methionine is a ____ amino acid

A

nonpolar/hydrophobic

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22
Q

phenylalanine is a ____ amino acid

A

nonpolar/hydrophobic

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23
Q

tryptophan is a _____ amino acid

A

nonpolar/hydrophobic

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24
Q

alanine has a ____ R chain

A

short

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25
Q

valine has a ____ R chain

A

short

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26
Q

leucine has a ____ R chain

A

short

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27
Q

isoleucine has a ____ R chain

A

short

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28
Q

phenylalanine has a _____ R chain

A

ring structure

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29
Q

tryptophan has a _____ R chain

A

6 side ring fused to a 5 side N structure

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30
Q

proline has a ____ R chain

A

unique cyclic

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31
Q

methionine has a ____ R chain

A

sulfur containing

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32
Q

There are _____ polar amino acids

A

8

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33
Q

glycine is a _____ amino acid

A

polar

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34
Q

serine is a _____ amino acid

A

polar

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35
Q

threonine is a _____ amino acid

A

polar

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36
Q

tyrosine is a _____ amino acid

A

polar

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37
Q

cysteine is a _____ amino acid

A

polar

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38
Q

asparagine is a _____ amino acid

A

polar

39
Q

glutamine is a _____ amino acid

A

polar

40
Q

histidine is a _____ amino acid

A

polar

41
Q

glycine has a ____ R group

A

simplest, H

42
Q

serine has a ____ R group

A

hydroxyl (OH)

43
Q

OH is what kind of group?

A

hydroxyl

44
Q

threonine has a _____ R group

A

hydroxyl (OH)

45
Q

tyrosine has a ____ R group

A

hydroxyl (OH)

46
Q

cysteine has a ____ R group

A

sulfur containing

47
Q

asparagine has a ____ R group

A

amide (NH2)

48
Q

glutamine has a ____ R group

A

amide (NH2)

49
Q

histidine has a _____ R group

A

amide

50
Q

____ is unique in that at pH above or at 7 it has normal structure but at pH below 7, the second nitrogen binds to an extra H+ and gives the R side chain a positive charge

A

histidine

51
Q

The sulfur R side chain group on cysteine is ____ reactive

A

highly

52
Q

What are the 2 acidic amino acids (have net neg charge at pH 7)

A

aspartic acid, glutamid acid

53
Q

How many acidic amino acids are there?

A

2

54
Q

the acidic amino acids what a ____ R group

A

carboxyl (COOH)

55
Q

What are the 2 basic amino acids (net pos charge at neutral pH)?

A

lysine, arginine

56
Q

the basic amino acids have a ____ R group

A

positively charged nitrogen group

57
Q

Hydroxylysine is a modified _____ found in _____

A

lysine, collagen

58
Q

Hydroxylysine has an added _____ compared to lysine

A

OH

59
Q

Acetyllysine is a modified ____ found in ____ ______

A

lysine, histone proteins

60
Q

thyroxine is 2 ______ and is found in ___ _____

A

tyrosines, thyroid hormone

61
Q

Thyroxine has added ___ _____ and lost other atoms

A

4 iodines

62
Q

Carboxyglutamic acid is modified ____ involved ____ _____

A

glutamic acids, blood clotting

63
Q

Carboxyglutamic acid has added 2 _____ ______

A

carboxyl groups

64
Q

Carboxyglutamic acid is found with the protein in blood clotting factors to ____ them

A

activate

65
Q

Acetyllysine has an added _____ linked through the amino group

A

acetyl

66
Q

Acetyllysine allowed for _____ _______ and the modification is later removed to allow histones to rebind to DNA

A

DNA seperation

67
Q

Acetyllysine ______ lysine to allow for DNA strand seperation

A

neutralized

68
Q

The cationic form of amino acids is at a ___ pH

A

low

69
Q

the _____ group is neutral when the amino acid is in cationic form

A

carboxyl

70
Q

the ____ group is positively charged when the amino acid is in cationic form

A

amino

71
Q

the ____ bound hydrogen is released when going from cationic form to zwitterion (neutral)

A

weakly bound

72
Q

The ____ group is negatively changed when the amino acid is in neutral/zwitterion form

A

carboxyl

73
Q

The ____ group is positively changed when the amino acid is in neutral/zwitterion form

A

amino

74
Q

The ____ group is negatively changed when the amino acid is in anionic form

A

carboxyl

75
Q

The ____ group is neutral when the amino acid is in anionic form

A

amino

76
Q

The amino acid is in ____ form when the pH is high

A

anionic

77
Q

The 1 positive and 1 negative charged group on the zwitterion atom makes it ______ (they cancel out)

A

neutral

78
Q

The net charge is _____ in the cationic form

A

positive (+1)

79
Q

The net charge is _____ in the anionic form

A

negative (-1)

80
Q

The overall charge of the amino acid is highly sensitive to _____

A

pH

81
Q

The most important reaction of amino acids is making a ________ _________

A

peptide bond

82
Q

A peptide bond is formed by the reaction of the ____ group of one amino acid and the _____ group of another

A

carboxyl (COO-), amino (NH3+)

83
Q

The reaction of forming a peptide bond results in the creation and loss of a ____ molecule

A

water

84
Q

CO-NH is a ____ bond

A

peptide/amide

85
Q

The result of a peptide bond formation has a ____-terminal end and a ____-terminal end

A

N, C

86
Q

The formation of a ____ ______ aides in the folding of protein chains, helps form loops, and stabilizes the 3D protein structure

A

disulfide bridge

87
Q

What are the three terms for having two possible configurations?

A

mirror-image isomers, enantiomers, chiral

88
Q

All proteins are naturally found in the ____ configuration

A

L

89
Q

The two mirror images are the ___ form and the ____ form

A

L (left/levo), D (dextro/right)

90
Q

The lab technique of separating amino acids or proteins is ___ ____ _______

A

ion exchange chromatography

91
Q

The ___ _____ charged amino acid is eluted first in the ion exchange chromatography

A

least positively

92
Q

The bead used in ion exchange chromatography is ___ charged

A

negatively

93
Q

The amino acid that can form a disulfide bridge is ______

A

cysteine

94
Q

If a protein is X amino acid residues in length, how many different amino acid sequences are possible?

A

20^X

BIOC3021 (25 decks)

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