20 Amino Acids Flashcards

1
Q

3 letter code: Glycine

A

Gly

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2
Q

1 letter code: Glycine

A

G

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3
Q

3 letter code: Alanine

A

Ala

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4
Q

1 letter code: Alanine

A

A

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5
Q

3 letter code: Valine

A

Val

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6
Q

1 letter code: Valine

A

V

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7
Q

3 letter code: Leucine

A

Leu

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8
Q

1 letter code: Leucine

A

L

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9
Q

3 letter code: Isoleucine

A

Ile

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10
Q

1 letter code: Isoleucine

A

I

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11
Q

3 letter code: Proline

A

Pro

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12
Q

1 letter code: Proline

A

P

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13
Q

3 letter code: Phenylalanine

A

Phe

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14
Q

1 letter code: Phenylalanine

A

F

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15
Q

3 letter code: Tyrosine

A

Tyr

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16
Q

1 letter code: Tyrosine

A

Y

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17
Q

3 letter code: Tryptophan

A

Trp

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18
Q

1 letter code: Tryptophan

A

W

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19
Q

3 letter code: Cysteine

A

Cys

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20
Q

1 letter code: Cysteine

A

C

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21
Q

3 letter code: Methionine

A

Met

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22
Q

1 letter code: Methionine

A

M

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23
Q

3 letter code: Serine

A

Ser

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24
Q

1 letter code: Serine

A

S

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25
Q

3 letter code: Threonine

A

Thr

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26
Q

1 letter code: Threonine

A

T

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27
Q

3 letter code: Asparagine

A

Asn

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28
Q

1 letter code: Asparagine

A

N

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29
Q

1 letter code: Glutamine

A

Q

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29
Q

3 letter code: Aspartic Acid

A

Asp

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29
Q

3 letter code: Glutamine

A

Gln

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30
Q

1 letter code: Aspartic Acid

A

D

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31
Q

3 letter code: Glutamic Acid

A

Glu

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32
Q

1 letter code: Lysine

A

K

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32
Q

1 letter code: Glutamic Acid

A

E

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33
Q

3 letter code: Lysine

A

Lys

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34
Q

3 letter code: Arginine

A

Arg

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35
Q

1 letter code: Arginine

A

R

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36
Q

3 letter code: Histidine

A

His

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37
Q

1 letter code: Histidine

A

H

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38
Q

Is glycine ionizable?

A

No

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39
Q

What amino acid has the smallest side chain?

A

Glycine

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40
Q

Is glycine polar or non-polar?

A

Technically neither, it’s too small

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41
Q

Why is glycine not a stereoisomer

A

because glycine doesn’t have 4 substituents

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42
Q

How is glycine related to the oral cavity

A

it is the most abundant amino acid in collagen which is everywhere in the oral cavity

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43
Q

Is alanine polar or non-polar?

A

non-polar, hydrophobic

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44
Q

Is valine polar or non-polar?

A

non-polar, hydrophobic

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45
Q

Is leucine polar or non-polar?

A

non-polar, hydrophobic

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46
Q

Is isoleucine polar or non-polar?

A

non-polar, hydrophobic

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47
Q

Is proline polar or non-polar?

A

non-polar, hydrophobic

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48
Q

What are the aromatic hydrocarbon side chains

A

Phenylalanine, Tyrosine, and Tryptophan

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49
Q

What is important to remember about aromatic hydrocarbon side chains

A

They don’t have fixed double bonds, they have resonance

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50
Q

Is phenylalanine polar or non-polar

A

non-polar, hydrophobic

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51
Q

Is tyrosine polar or non-polar?

A

has both polar and non-polar characteristics, intermediate

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52
Q

is tryptophan polar or non-polar

A

has both polar and non-polar characteristics, intermediate

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53
Q

Which side chains contain sulfur

A

Cysteine and Methionine

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54
Q

What are the non-aromatic hydrocarbon side chains

A

Alanine, Valine, Leucine, Isoleucine, Proline

55
Q

Is cysteine polar or non-polar

A

Doesn’t fit either

56
Q

Is methionine polar or non-polar

A

Non-polar and hydrophobic

57
Q

What is important about Methionine

A

It is the amino acid that’s used to initiate the synthesis of all proteins specified by the genetic code

58
Q

What are the polar uncharged side chains

A

Serine, Threonine, Asparagine, Glutamine

59
Q

Is serine polar or non-polar

A

Polar, hydrophilic

60
Q

Is threonine polar or non-polar

A

polar, hydrophilic

61
Q

Is asparagine polar or non-polar

A

polar, hydrophilic

62
Q

What is special about asparagine

A

it has an amide

63
Q

What are the polar charged side chains

A

Aspartic acid, glutamic acid, lysine, arginine, histidine

64
Q

Is glutamine polar or non-polar

A

polar, hydrophilic

65
Q

What is the pKa of Aspartic acid

A

~4

66
Q

Is glutamic acid polar or non-polar

A

polar, hydrophilic

67
Q

What amino group does lysine have

A

Epsilon amino group

68
Q

Is lysine polar or non-polar

A

polar, hydrophilic

69
Q

Is arginine polar or non-polar

A

polar, hydrophilic

70
Q

Is histidine polar or non-polar

A

polar, hydrophilic

71
Q

What is special about histidine

A

It has an imidazole

72
Q

What is special about arginine

A

It has a guanidinium

73
Q

Is glycine ionizable?

A

No

74
Q

Is alanine ionizable?

A

No

75
Q

Is valine ionizable?

A

No

76
Q

Is leucine ionizable?

A

No

77
Q

Is proline ionizable?

A

No

78
Q

Is isoleucine ionizable?

A

No

79
Q

Is phenylalanine ionizable?

A

No

80
Q

Is Tyrosine ionizable?

A

Yes

81
Q

Is tryptophan ionizable?

A

No

82
Q

Is cysteine ionizable?

A

Yes

83
Q

Is methionine ionizable?

A

No

84
Q

Is serine ionizable?

A

No

85
Q

Is threonine ionizable?

A

No

86
Q

Is asparagine ionizable?

A

No

87
Q

Is glutamine ionizable?

A

No

88
Q

Is aspartic acid ionizable?

A

Yes

89
Q

Is glutamic acid ionizable?

A

Yes

90
Q

Is lycine ionizable?

A

Yes

91
Q

Is arginine ionizable?

A

Yes

92
Q

Is histidine ionizable?

A

Yes

93
Q

x

A

x

94
Q

x

A

x

95
Q

What state is lysine at physiological pH

A

acidic

96
Q

x

A

x

97
Q

x

A

x

98
Q

x

A

x

99
Q

Phospholipids can have protein access channels, explain

A

You can put in protein access channels that will move things in and out in a regulated fashion –> you can modulate the fluidity of these membranes

100
Q

Why can’t phospholipids form a micelle

A

Because they are too bulky so we get a bilayer structure instead

101
Q

Describe the aqueous phases of the phospholipid bilayers

A

The aqueous phases are on inside and outside of a membrane

The chemical barrier of the bilayer prevents these 2 fluids from mixing

102
Q

Phospholipids are

A

amphipathic

103
Q

Is phosphate polar or non-polar

A

polar

104
Q

Will polar molecules pass through phospholipid bilayers?

A

No

105
Q

What barriers are phospholipids great at being?

A

They are great chemical barriers but not rigid enough to be physical barriers

106
Q

Explain phospholipid membrane movement

A

The membranes have an outer and inner leaflet, the phospholipids can move 3D within a leaflet laterally

Changing the properties can slow down (rigid) or speed up (increase the fluid) their movement

They cannot flip flop from 1 side to the other

107
Q

Discuss the fluid mosaic model of biological membranes

A

Proteins will jiggle its way in the membrane and the bilayer will make space for the protein via its fluidity

Proteins can either be internal/transmembrane (with a polar interior channel that allows things to go through) or peripheral that has its tail sitting in the membrane (could be a defense membrane)

Often these proteins need to be able to move and aggregate with other proteins to perform these defense functions

108
Q

Explain how fatty acids and soap work

A

Fatty acids in soap will find hydrophobic locations on the hand aka the virus lipid envelope and disrupt it.

The phospholipids now have somewhere else to go other than the aqueous environment = embed within micelles

So we are disrupting the virus’ ability to infect us like dissolves like

109
Q

What is the only amino acid that has a Nitrogen that makes 2 bonds with carbon?

A

Proline (it has an imino acid)

110
Q

What is the terminology for the N group on the left side of amino acids

A

L- amino acid

111
Q

What is the terminology for the N group on the right side of amino acids

A

D-amino acid

112
Q

General properties of amino acids

A

making 4 bonds with carbons

4 different substituent groups attached to Carbon = chiral

Chiral - mirror images but not superimposable

L stereoisomer found only in proteins!!

113
Q

What are the “wonders of Cysteine”

A

it has a sulfur, thiol group, and can form disulfide bonds

it is also ambiguous regarding polar or non-polarity

it participates in many biological oxidation/reduction reactions

only side chains of a protein that can form a covalent bond

114
Q

pKa of Cysteine

A

~8

115
Q

pH < pKa ?

A

acid

116
Q

pH > pKa

A

base

117
Q

pH = pKa

A

1/2

118
Q

What is phosphorylation and why is it used

A

Phosphate is an acid and will react with the OH and forms phosphate ester

Used to regulate a protein’s function

119
Q

What does neutral side mean regarding amino acids?

A

the side chain is not ionizable

120
Q

What is a Zwitterion

A

+ and - charges can balance each other

121
Q

low pH means what regarding state and charge?

A

all groups in acid state

below pH 2

122
Q

high pH means what regarding state and charge

A

everything base state and it becomes neutral

carboxyl group loses its proton and becomes negatively charged -1

above pH 10

123
Q

how do you find the pI

A

you take the average of the like charges

ex: 2 + 6 / 2

124
Q

What pKa should be used when asked the pKa of a carboxyl group found on the alpha carbon of a free amino acid

A

pKa of 2

125
Q

what pKa should be used at any other time for a carboxyl group besides when carbon of a free amino acid is on one

A

pKa of 4

126
Q

What pKa is influenced by the environment

A

imidazole, 6
amino groups, 10
phenol, 10

127
Q

Properties of Tyrosine

A

aromatic ring with a hydroxyl group

can ionize if pH is high enough

can delocalize extra electron

neutral at physiological pH

128
Q

Discuss electron delocalization and tyrosine

A

electron delocalization within the aromatic ring stabilizes the ionized species and reduces pK of Tyrosine relative to Serine

129
Q

alpha-carboxyl approximate pK

A

2

130
Q

side chain carboxyl pK

A

4

131
Q

imidazole pK

A

6

132
Q

alpha and side chain amino groups pK

A

10

133
Q

phenol pK

A

10

134
Q

Guanidinium pK

A

12

135
Q

Explain guanidinium and its net charge delocalization

A

The pK of 12 basically means it will be in acid state and be +1

136
Q

Peptide bond formation is thermodynamically ?

A

Unfavorable so it won’t happen spontaneously

137
Q

Structure gives rise to

A

Function

138
Q

Proteins with similar charge to mass ratios will migrate at the ?

A

same rate in an electric field

139
Q

limitations to simple electrophoresis

A

Size

Large proteins = more friction