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Biochemistry LEC > Module 4: Amino Acids > Flashcards

Module 4: Amino Acids Flashcards

1
Q

polymers of amino acids, with each amino acid residue joined to its neighbor by a specific type of covalent bond.

A

Proteins

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2
Q

The term _______ reflects the loss of the elements of water when one amino acid is joined to another

A

“residue”

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3
Q

How many different amino acids are commonly found in proteins

A

20

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4
Q

the first to be discovered in 1806

A

Asparagine

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5
Q

the last of the 20 to be found in 1938

A

Threonine

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6
Q

was first found in asparagus

A

Aspargine

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7
Q

in wheat gluten

A

glutamate

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8
Q

was first isolated from cheese (its name is derived from the Greek tyros, “cheese”)

A

tyrosine

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9
Q

(Greek glykos,“sweet”) was so named because of its sweet taste

A

glycine

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10
Q

Proteins are naturally-occurring, unbranched polymer in which the monomer units are ______

A

Amino Acids

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11
Q

what percentage of a cell’s overall mass do Amino Acids account for?

A

15%

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12
Q

What elements make up the composition of proteins?

A

Carbon, Hydrogen, Nitrogen, Oxygen, Sulfur

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13
Q

an organic compound that contains both
an amino (-NH2) group and a carboxyl group ((-COOH)

A

amino acid

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14
Q

The amino acid found in CHON are always

A

α-amino acid

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15
Q

an amino acid which the amino group and the carboxyl group are attached to the α-carbon atom

A

α-amino acid

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16
Q

the side chain is also called

A

R group

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17
Q

The R group is called the

A

side chain

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18
Q

how many possible stereoisomers can amino acids have

A

2

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19
Q

Are the following non-polar, acidic, basic, or neutral?

Alanine, Glycine, Isoleucine, Leucine, Methionine, Proline, Valine

A

NON-POLAR

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20
Q

Are the following non-polar, acidic, basic, or neutral?

Aspartic Acid, Glutamic Acid

A

ACIDIC

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21
Q

Are the following non-polar, acidic, basic, or neutral?

Arginine, Histidine, Lysine

A

BASIC

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22
Q

Are the following non-polar, acidic, basic, or neutral?

Asparagine, Cysteine, Glutamine, Serine, Threonine, Tyrosine

A

NEUTRAL

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23
Q

What type of amino acids are Phenylalanine & Tryptophan?

A

Non-Polar Aromatic

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24
Q

has the simplest structure. Although it is formally nonpolar, it’s very small side chain makes no real contribution to hydrophobic interactions

A

Glycine

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25
Q

________ has an aliphatic side chain with a distinctive cyclic structure. The secondary amino (imino) group of ________ residues is held in a rigid conformation that reduces the structural flexibility of polypeptide regions containing ________

A

Proline

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26
Q

__________ one of the two sulfur containing amino acids, has a nonpolar thioether group in its side chain

A

Methionine

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27
Q

Can be viewed as a benzyl group
substituted for the methyl group of
alanine, or a phenyl group in place of terminal H of alanine

A

Phenylalanine

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28
Q

The –OH group can form H-bonds, an important functional group in some enzymes

A

Tyrosine

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29
Q

Is a borderline member of aromatic R groups because water can
weakly interact through
H-bonding with the NH ring

A

Tryptophan

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30
Q

2nd primary amino group at terminal position on its aliphatic chain

A

Lysine

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31
Q

Positively charged guanidino group. The guanidine group on side chain contains 3-Natoms of which 2 can easily undergo condensation reaction with carbonyl compounds

A

Arginine

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32
Q

Has imidazole group. Five membered
heterocyclic moiety.

A

Histidine

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33
Q

–carboxyl group has lost its acidic hydrogen atom

A

Negatively Charged (Acidic) R Groups

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34
Q

more polar than phenylalanine due to –OH of tyr and N of try indole ring

A

Tyrosine & Tryptophan

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35
Q

what groups are nonpolar and hydrophobic

A

R groups

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36
Q

what amino acids are positively charged R groups

A

Lysine, Arginine, Histidine

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37
Q

what amino acids are negatively charged R groups

A

Aspartate and Glutamate

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38
Q

what amino acids are polar, uncharged R groups

A

Serine, threonine, cysteine, Asparagine and Glutamine

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39
Q

the only standard amino acid that has a side chain that contains a sulfhydryl group

A

Cysteine

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40
Q

What are the two types of amino acids

A

essential and non essential

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41
Q

what type of amino acids is not produced in the body

A

essential

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42
Q

what type of amino acids are produced by the body

A

non-essential

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43
Q

What amino acids are essential

A

Phenylanine, Valine, Threonine, Tryptophan, Isoleucine, Methionine, Histidine, Arginine, Leucine, Lysine

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44
Q

What amino acids are non-essential

A

Alanine, Aspartic Acid, Glutamic Acid, Glutamine, Cysteine, Glycine, Tyrosine, Proline, Serine

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45
Q

The amino acids found in nature as well as in proteins are

A

L isomers

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46
Q

The –NH2 group is in a ________ position

A

horizontal

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47
Q

_______ and ________ possess two chiral centers

A

Isoleucine and Threonine

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48
Q

usually formed by an enzyme-facilitated reaction on a common amino acid after that amino acid has been incorporated into a protein structure

A

Uncommon Amino Acids

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49
Q

Derivative of 4 Lys residues

A

Desmosine

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50
Q

found in elastin

A

Isodesmosine

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51
Q

constituent of myosin

A

6-N-methyllysine

52
Q

found in collagen

A

hydroxyproline and
hydroxylysine

53
Q

found in prothrombin

A

𝛾-carboxyglutamate

54
Q

Compounds like the basic structure of amino acids, but do not
occur in proteins

A

Non-Standard Amino Acids

55
Q

Found in coenzyme A

A

β-alanine

56
Q

found in bile acids

A

Taurine

57
Q

intermediates in urea cycle

A

ornithine and citrulline

58
Q

thyroid hormones synthesized from
tyrosine

A

thyroxine (T4) and tri-iodo thyronine (T3)

59
Q

a neurotransmitter produced from
glutamic acid

A

𝛾-aminobutyric acid (GABA)

60
Q

End-product of pyrimidine metabolism

A

β-amino isobutyric acid

61
Q

intermediate in heme synthesis

A

δ-aminolevulinic acid (δ-ALA)

62
Q

methyl donor formed from L-methionine

A

S-adenosyl methionine (SAM)

63
Q

a precursor of melanin pigment

A

3,4-dihydroxyphenylalanine
(DOPA)

64
Q

constituents of bacterial cell walls

A

D-glutamic acid and D-alanine

65
Q

found in certain antibiotics, e.g., gramicidin-S, Actinomycin-D

A

D-amino acids

66
Q

have been found in brain tissue

A

D-aspartate and D-serine

67
Q

– Contains an essential dietary micronutrient- selenium) as a
constitutive component.

A

Selenocysteine

68
Q

found in mammalian blood. It has an antioxidant function, and its concentration falls in selenium deficiency

A

Selenoprotein P

69
Q

− 22nd amino acid
− used for biosynthesis of proteins in some methanogenic archaea and bacteria

A

Pyrrolysine (Pyl, O)

70
Q

Some amino acids are converted to carbohydrates and are called as

A

glucogenic amino acids

71
Q

forms hormones such as thyroid hormones (T3 and T4), epinephrine and
norepinephrine, and a pigment called
melanin

A

Tyrosine

72
Q

can synthesize a vitamin called niacin Formed serotonin

A

Tryptophan

73
Q

synthesize creatine

A

Glycine, arginine and methionine

74
Q

help in synthesis of bile salts

A

Glycine and cysteine

75
Q

Synthesize glutathione

A

Glutamate, cysteine, & glycine

76
Q

Changes histamine on decarboxylation

A

Histidine

77
Q

Is used for the synthesis of heme

A

Glycine

78
Q

Pyrimidine uses these amino acids for their
synthesis

A

Aspartate & Glutamine

79
Q

Purine synthesis

A

Glycine, aspartic acid, glutamine, & serine

80
Q

In neutral solution, the –COOH group of an amino acid donates a proton to the –NH2 of the same amino acid. This is called an ________ reaction

A

internal acid–base reaction

81
Q

– a molecule with positive and negative charges on the same molecule, but has no net charge

A

zwitterions

82
Q

Substances that have a dual (acid-base) nature are _____ and often called ______

A

amphoteric, ampholytes

83
Q

pH at which an amino acid exist primarily in its zwitterion form (net charge is zero)

A

Isoelectric point (pI)

84
Q

True or False?
At isoelectric points, amino acids are attracted towards an applied electric field
because they carry net zero charge.

A

False, amino acids are NOT attracted towards an applied electric field
because they carry net zero charge

85
Q

are composed of only a small number of
amino acids joined as peptide bonds

A

Peptides

86
Q

made up of two amino acids

A

Dipeptides

87
Q

made up of three amino acid

A

Tripeptides

88
Q

refers to peptides with 10 to 20 amino acid residues

A

Oligopeptide

89
Q

a long unbranched chain of amino acids

A

Polypeptide

90
Q

True or False?
Under proper conditions, amino acids can bond together to produce an unbranched chain of amino acids

A

True

91
Q

if an amino acid chain has 5 amino acids how many peptide bonds exist?

A

4 peptide bonds

92
Q

The structure of peptides is represented beginning with the amino acid whose amino group is free

A

N-terminal end

93
Q

The other end contains a free carboxyl
group and is the

A

C-terminal end

94
Q

The amino acid at one end of amino
acid sequence has a free _____ group,
and the amino acid at the other end with
a free ______ group

A

H3N+, COO-

95
Q

The individual amino acids within a peptide chain are called

A

amino acid residues

96
Q

– best-known peptide hormones: oxytocin and vasopressin
– produced by the pituitary gland
– nonapeptide (nine amino acid residues) with six of the residues held in the form of a loop by a disulfide bond formed between two cysteine residues. Differ in the amino acid present in positions 3 and 8 of the peptide chain

A

Small peptide hormones

97
Q
  • Enkephalins are pentapeptide neurotransmitters produced by the brain and bind receptors within the brain
  • help reduce pain
A

Small peptide neurotransmitters

98
Q

Best-known enkephalins

A
  1. Met-enkephalin: Tyr–Gly–Gly–Phe–Met
  2. Leu-enkephalin: Tyr–Gly–Gly–Phe–Leu
99
Q

The action of the prescription painkillers morphine and codeine is based on the actions of __________

A

enkephalins

100
Q

Unusual structural feature – Glu is bonded to Cys through the side-chain carboxyl group

A

Small peptide antioxidants

101
Q

− dipeptide sold under trade names Equal and Nutrasweet
− ~180x as sweet as sucrose

A

Aspartame (Asp-Phe)

102
Q

ONE LETTER: A
THREE LETER: Ala

A

Alanine

103
Q

ONE LETTER: R
THREE LETTER: Arg

A

Arginine

104
Q

ONE LETTER: N
THREE LETTER: Asn

A

Asparagine

105
Q

ONE LETTER: D
THREE LETTER: Asp

A

Aspartic acid

106
Q

ONE LETTER: C
THREE LETTER: Cys

A

Cysteine

107
Q

ONE LETTER: Q
THREE LETTER: Gln

A

Glutamine

108
Q

ONE LETTER: E
THREE LETTER: Glu

A

Glutamic Acid

109
Q

ONE LETTER: G
THREE LETTER: Gly

A

Glycine

110
Q

ONE LETTER: H
THREE LETTER: His

A

Histidine

111
Q

ONE LETTER: I
THREE LETTER: Ile

A

Isoleucine

112
Q

ONE LETTER: L
THREE LETTER: Leu

A

Leucine

113
Q

ONE LETTER: K
THREE LETTER: Lys

A

Lysine

114
Q

ONE LETTER: M
THREE LETTER: Met

A

Methionine

115
Q

ONE LETTER: F
THREE LETTER: Phe

A

Phenylalanine

116
Q

ONE LETTER: P
THREE LETTER: Pro

A

Proline

117
Q

ONE LETTER: S
THREE LETTER: Ser

A

Serine

118
Q

ONE LETTER: T
THREE LETTER: Thr

A

Threonine

119
Q

ONE LETTER: W
THREE LETTER: Typ

A

Tryptophan

120
Q

ONE LETTER: Y
THREE LETTER: Tyr

A

Tyrosine

121
Q

ONE LETTER: V
THREE LETTER: Val

A

Valine

122
Q

ONE LETTER: O
THREE LETTER: Pyl

A

Pyrrolysine

123
Q

ONE LETTER: U
THREE LETTER: Sec

A

Selenocysteine

124
Q

ONE LETTER: B
THREE LETTER: Asx

A

Aspartic acid or Asparagine

125
Q

ONE LETTER: Z
THREE LETTER: Glx

A

Glutamic acid or Glutamine

Biochemistry LEC (8 decks)

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