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BHCM218 > Module 01 - Section 02 > Flashcards

Module 01 - Section 02 Flashcards

Introduction to Amino Acids

1
Q

What is the difference between peptide, polypeptide and protein?

A

Often used interchangeably, but generally;
peptide = <10 amino acids
polypeptide = <100 amino acids
polypeptide chain = any size
protein= large macromolecule that can be composed of one or more polypeptide chains

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2
Q

What distinguishes an amino acid from another?

A

The R-group, also called side chain

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3
Q

How are Amino Acids classified? (2+5)

A

(1) Nonpolar
(a) Aliphatic
(b) Aromatic
(2) Polar
(a) Uncharged
(b) Negatively charged
(c) Positively charged

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4
Q

What are the Aliphatic amino acids? (7)

A

GAVLIMP

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

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5
Q

What are the Aromatic amino acids? (3)

A

Phenilalanine, Tryptophan, Tyrosine

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6
Q

What are the Uncharged Amino acids? (5)

A

STNCQ (“Stinky Q”)

Cysteine, Asparagine, Glutamine, Serine, Threonine

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7
Q

What are the negatively charged amino acids? (2)

A

Aspartate, Glutamate

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8
Q

What are the positively charged amino acids? (3)

A

Lysine, Arginine, Histidine

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9
Q

Which amino acid is the smallest?

A

Glycine

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10
Q

Which nonpolar aliphatic contribute the least to hydrophobic effects?

A

Glycine

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11
Q

Which amino acids are isomers of each other?

A

Leucine and Isoleucine, they have the same number of carbon and hydrogen atoms but are arranged differently

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12
Q

Which amino acids have simple hydrocarbons chains? (4)

A

Alanine, Valine, Leucine, Isoleucine

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13
Q

3-letter abre: Gly

A

Glycine

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14
Q

1-letter: G

A

Glycine

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15
Q

3-letter: Ala

A

Alanine

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16
Q

1-letter: A

A

Alanine

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17
Q

3-letter: Val

A

Valine

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18
Q

1-letter: V

A

Valine

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19
Q

3-letter: Leu

A

Leucine

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20
Q

1-letter: L

A

Leucine

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21
Q

3-letter: Ile

A

Isoleucine

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22
Q

1-letter: I

A

Isoleucine

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23
Q

Which amino acid contains a thioether group in its side chain?

A

Methionine

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24
Q

3-letter: Met

A

Methionine

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25
Q

1-letter: M

A

Methionine

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26
Q

Which is the only amino acid whose side chain connects to its amino group?

A

Proline

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27
Q

What is special about proline?

A

Its side-chain is connected to its amino group. The resulting 5-membered ring causes proline to be very rigid and thus limits its possible conformations

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28
Q

3-letter: Pro

A

Proline

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29
Q

1-letter: P

A

Proline

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30
Q

3-letter: Phe

A

Phenylalanine

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31
Q

1-letter: F

A

Phenylalanine

32
Q

3-letter: Tyr

33
Q

1-letter: Y

34
Q

3-letter: Trp

A

Tryptophan

35
Q

1-letter: W

A

Tryptophan

36
Q

Which is the most hydrophobic of the Aromatic Amino Acids?

A

Phenylalanine

37
Q

Which Aromatic Amino acids can form hydrogen bonds? (2) which moieties are involved?

A

Tyrosine, Hydroxyl group -OH

Tryptophan, Nitrogen

38
Q

Which Amino acids are able to absorb UV light?

A

Aromatic Amino Acids – phenylalanine less than tryptophan and tyrosine

39
Q

Which property of which amino acids is used by researches in the characterization of proteins?

A

Absorption of 280nm wavelength light by the aromatic rings of aromatic amino acids

40
Q

Which type of amino acids can interact extensively with water, or with atoms in other side chains through hydrogen bonds?

A

Polar uncharged amino acids

41
Q

3-letter: Cys

42
Q

1-letter: C

43
Q

3-letter: Asn

A

Asparagine

44
Q

1-letter: N

A

Asparagine

45
Q

3-letter:Gln

46
Q

1-letter: Q

47
Q

3-letter: Ser

48
Q

1-letterL S

49
Q

3-letter: Thr

50
Q

1-letter: T

51
Q

Which amino acid residues can be oxidized to form a disulfide bond?

52
Q

Which Amino Acid contains a sulfhydryl group?

53
Q

What bond connects two regions of one or more polypeptide chains within a protein and acts as a molecular cross-brace to enhance protein stability?

A

Disulfide bond

54
Q

What is a nucleophile?

A

Reactant that provides a pair of electrons to form a new covalent bond

55
Q

Name the 2 roles of Cysteine in proteins

A

(1) Enhance protein stability through disulfide bonds

(2) Important in catalytic functions of many enzymes, as the deprotonated -SH is a good nucleophile

56
Q

Which amino acids’ side chains contain an amide group that can act as both a donor or acceptor of electrons? (2)

A

Asparagine & Glutamine

57
Q

Describe the side Chains of Asparagine and Glutamine (2)

A

They contain an amide group that can act as an electron donor and acceptor and also contain a carbonyl group (C=O) that can participate in hydrogen bonding

58
Q

Describe the side chains of Serine and Threonine (2)

A

They have an hydroxyl group capable of forming hydrogen bonds. They can also be phosphorylated by kinases, resulting in protein modifications.

59
Q

Polar negatively charged Amino Acids (2)

A

Apartate, Glutamate

60
Q

3-letter: Asp

61
Q

1-letter: D

62
Q

3-letter: Glu

63
Q

1-letter: E

64
Q

Describe the side chains of aspartate and glutamate

A

Contains a carboxyl group and therefore carry a negative charge at pH 7.0

65
Q

What are the 3 polar, positively charged amino acids?

A

Lysine, Arginine, Histidine

66
Q

3-letter: Lys

67
Q

1-Letter: K

68
Q

3-letter: Arg

69
Q

1-letter: R

70
Q

3-letter: His

71
Q

1-letter: H

72
Q

Which amino acid contains a side chain amino group?

73
Q

Which amino acid contains a side chain guanidinium group?

74
Q

Which Amino acids contains an imidazole group?

75
Q

Where do charged amino acids tend to be located?

A

The exterior of proteins, in contact with water, because they are very hydrophilic and able to make hydrogen bonds with water

76
Q

Why are charged amino acids important to enzyme function?

A

They tend to be located in the active, because they are very hydrophilic and their ability to form hydrogen bonds and ionic interactions with oppositely charged molecules (like other amino acids and metal ions)

BHCM218 (24 decks)

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