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BIOCHEM > Amino Acids > Flashcards

Amino Acids Flashcards

1
Q

What are the structures of typical amino acids found in proteins?

A

Carbon atom (a-carbon atom) covalently linked to:

(a) amino group (-NH2)
(b) carboxyl group (-COOH)
(c) variable side chain (R-group)
(d) hydrogen (-H)

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2
Q

How many amino acids are there?

A

20

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3
Q

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

A

(a) amino group (-NH2)
(b) carboxyl group (-COOH)
(c) variable side chain (R-group)
(d) hydrogen (-H)

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4
Q

At physiological pH, the amino group is _______

A

Protonated. (-NH3+)

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5
Q

At physiological pH, the carboxyl group is ______

A

Unprotonated. (-COOH-)

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6
Q

What makes up a tetrahedral amino acid structure?

A
  1. 4 equilateral triangles
  2. Alpha carbon in the middle
  3. 4 vertices (amino group, carboxyl group, R side chain, alpha carbon)
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7
Q

How many Nonpolar/Hydrophobic Amino Acids are there?

A

8

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8
Q

What are the 8 nonpolar/hydrophobic amino acids?

A

Alanine (Ala)
Valine (Val)
Leucine (Leu)
Isoleucine (Ile)
Proline (Pro)
Methionine (Met)
Phenylalanine (Phe)
Tryptophan (Trp)

Alaska Values Leuding Illegal Pro Meth Phetanyl Trp

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9
Q

ALA

A

Alanine

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10
Q

VAL

A

Valine

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11
Q

LEU

A

Leucine

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12
Q

ILE

A

Isoleucine

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13
Q

PRO

A

Proline

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14
Q

MET

A

Methionine

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15
Q

PHE

A

Phenylalanine

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16
Q

TRP

A

Tryptophan

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17
Q

A

A

Alanine

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18
Q

V

A

Valine

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19
Q

L

A

Leucine

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20
Q

I

A

Isoleucine

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21
Q

P

A

Proline

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22
Q

M

A

Methionine

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23
Q

F

A

Phenylalanine

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24
Q

W

A

Tryptophan

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25
Q

Why are amino acids nonpolar/hydrophobic?

A

They are made of just carbons & hydrogens. Either in forms of chain, cyclic structures, or linear

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26
Q

Alanine (Ala, A) R chain

A

alkyl chain R group
(linear chain of carbon & hydrogens)
(short with branches)

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27
Q

Valine (Val, V) R chain

A

alkyl chain R group
(linear chain of carbon & hydrogens)
(short with branches)

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28
Q

Leucine (Leu, L) R chain

A

alkyl chain R group
(linear chain of carbon & hydrogens)
(short with branches)

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29
Q

Isoleucine (Ile, I) R chain

A

alkyl chain R group
(linear chain of carbon & hydrogens)
(short with branches)

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30
Q

Proline (Pro, P) R chain

A

unusual cyclic structure

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31
Q

Methionine (Met,M) R chain

A

sulfur containing

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32
Q

Phenylalanine (Phe, F) R chain

A

aromatic
(6 sided ring structure)

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33
Q

Tryptophan (Trp, W) R chain

A

aromatic
(6 sided ring structure)

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34
Q

What makes prolines structure unique?

A

It has two linkage points to the central carbon from the R-Side chain

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35
Q

How many polar/hydrophilic amino acids are there?

A

8

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36
Q

What are the polar/hydrophilic amino acids?

A

Asparagine (Asn)
Glycine (Gly)
Histidine (His)
Glutamine (Gln)
Threonine (Thr)
Serine (Ser)
Tyrosine (Tyr)
Cysteine (Cys)

As Gly hits glutes, threo seriously types cysts

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37
Q

Gly

A

Glycine

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38
Q

Ser

A

Serine

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39
Q

Threonine

A

Thr

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40
Q

Tyr

A

Tyrosine

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41
Q

Asn

A

Asparagine

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42
Q

Gln

A

Glutamine

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43
Q

His

A

Hisidine

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44
Q

G

A

Glycine

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45
Q

S

A

Serine

46
Q

T

A

Threonine

47
Q

Y

A

Tyrosine

48
Q

C

A

Cysteine

49
Q

N

A

Asparagine

50
Q

Q

A

Glutamine

51
Q

H

A

Histidine

52
Q

Glycine (Gly, G) R chain

A

Simplest R group (H)
* Doesn’t fit with polar or nonpolar *

53
Q

Threonine (Thr, T) R chain

A

Hydroxyl (OH) at end of R side chain
Branched

53
Q

Serine (Ser, S) R chain

A

Hydroxyl (OH) at end of R side chain
Linear

54
Q

Tyrosine (Tyr, Y) R chain

A

Hydroxyl (OH) at end of R side chain
Ring

55
Q

Cysteine (Cys, C)

A

Sulfur containing (SH)

56
Q

Asparagine (Asn, N)

A

Amide in R group (NH2)
Linear

57
Q

Glutamine (Gln, Q)

A

Amide in R group (NH2)
Branched

58
Q

Histidine (His, H)

A

Amide in R group (NH2)
Ring

59
Q

What are the R side chains of polar amino acids?

A

-OH -NH or -SH

60
Q

What are the R side chains of nonpolar amino acids?

A

-CH2 -CH3 - S

61
Q

How many acidic amino acids are there?

A

2

62
Q

What are the acidic amino acids?

A

Aspartic Acid (Asp, D)
Glutamic Acid (Glu, E)

63
Q

Aspartic acid (Asp, D) R chain

A

carboxyl (COOH) in R group

64
Q

Glutamic Acid (Glu, E)

A

carboxyl (COOH) in R group

65
Q

What does acidic amino acid mean?

A

Net negative charge at PH 7.0

66
Q

How many basic amino acids are there?

A

2

67
Q

What are the basic amino acids?

A

Lysine (Lys,K)
Arginine (Arg, R)

68
Q

Lysine (Lys,K) R chain

A

positively charged nitrogen-containing

69
Q

Arginine (Arg, R) R chain

A

positively charged nitrogen-containing

70
Q

What does basic amino acid mean?

A

net positive charge at neutral PH

71
Q

What are the 3 groups in the charged amino acids?

A
  • COO-
  • NH3+
    = NH2+
72
Q

Hydroxylysine is a modified ____ found in ____

A

lysine, collagen

73
Q

Acetyllysine is a modified ____ found in _____

A

lysine, histone proteins

74
Q

Thyroxine has added ____ and lost other atoms

A

4 iodines

75
Q

Carboxyglutamic acid is modified ____ involved in ____

A

glutamic acids, blood clotting

76
Q

Carboxyglutamic acid has two added ___

A

carboxyl groups

77
Q

Thyroxine makes ____

A

thyroid hormones

78
Q

Acetyllysine has an added ___ linked through the amino acid

A

acetyl

79
Q

Acetyllysin allowed for ___ and the modification is later removed to allow histones to rebind to DNA

A

DNA seperation

80
Q

Acetyllysin ____ lysine to allow for DNA strand seperation

A

neutralized

81
Q

The cationic form of an amino acid is at ___ pH

A

low

82
Q

What group is neutral when the amino acid is in cationic form?

A

carboxyl

83
Q

What group is positively charged when the amino acid is in cationic form?

A

amino

84
Q

What is released when going from cationic form to zwitterion form (neutral)?

A

H+

85
Q

What is negatively charged when the amino acid is in neutral/zwitterion form?

A

carboxyl

86
Q

What group is positively charged when the amino acid is in neutral/zwitterion form?

A

amino

87
Q

What is lost when going from zwitterion form to anionic form?

A

H+

88
Q

What group is negatively charged in anionic form?

A

carboxyl

89
Q

What group is neutral in anionic form?

A

amino

90
Q

Charge of cationic form

A

+1

91
Q

pH of cationic form

A

pH = 1

92
Q

Charge of zwitterion form

A

0

93
Q

pH of zwitterion form

A

pH = 7

94
Q

Charge of anionic form

A

-1

95
Q

pH of anionic form

A

pH = 13

96
Q

The 1 + and 1 - charged groups on the zwitterion atom makes it ______

A

neutral

97
Q

How is a peptide bond formed?

A

Reaction of the
1. carboxyl group of one amino acid
&
2. amino group of another

98
Q

Reaction of forming a peptide bond results in the ___ of a water molecule

A

water

99
Q

CO-NH is a ____ bond

A

peptide/amide

100
Q

Formation of a peptide bond

A
  1. Two amino acids
  2. Removal of a water molecule
  3. Formation of the CO-NH
101
Q

What are the two terminal ends of peptide bonds?

A
  1. N (amino end)
  2. C (carboxyl end)
102
Q

What are two reactions of amino acids

A
  1. peptide bond
  2. disulfide bridge
103
Q

Disulfide bridges involve the _ __ ____ of an amino acid

A

R side chain

104
Q

What does the formation of a disulfide bridge hekp with?

A

Folding of protein chains
Forms loops
Stabilizes the 3D protein structure

105
Q

What configuration are proteins naturally in?

A

L

106
Q

Are disulfide bridges essential?

A

NO

107
Q

Lab technique of seperating amino acids/proteins

A

Ion exchange chromatography

108
Q

What amino acid can form a disulfide bridge?

A

Cysteine

109
Q

Bead used in ion exchange chromatography is ____

A

negatively charged

BIOCHEM (16 decks)

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