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BHCM218 > Module 01 - Section 02 > Flashcards

Module 01 - Section 02 Flashcards

Introduction to Amino Acids (76 cards)

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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
1-letter: M
Methionine
26
Which is the only amino acid whose side chain connects to its amino group?
Proline
27
What is special about proline?
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
28
3-letter: Pro
Proline
29
1-letter: P
Proline
30
3-letter: Phe
Phenylalanine
31
1-letter: F
Phenylalanine
32
3-letter: Tyr
Tyrosine
33
1-letter: Y
Tyrosine
34
3-letter: Trp
Tryptophan
35
1-letter: W
Tryptophan
36
Which is the most hydrophobic of the Aromatic Amino Acids?
Phenylalanine
37
Which Aromatic Amino acids can form hydrogen bonds? (2) which moieties are involved?
Tyrosine, Hydroxyl group -OH | Tryptophan, Nitrogen
38
Which Amino acids are able to absorb UV light?
Aromatic Amino Acids -- phenylalanine less than tryptophan and tyrosine
39
Which property of which amino acids is used by researches in the characterization of proteins?
Absorption of 280nm wavelength light by the aromatic rings of aromatic amino acids
40
Which type of amino acids can interact extensively with water, or with atoms in other side chains through hydrogen bonds?
Polar uncharged amino acids
41
3-letter: Cys
Cysteine
42
1-letter: C
Cysteine
43
3-letter: Asn
Asparagine
44
1-letter: N
Asparagine
45
3-letter:Gln
Glutamine
46
1-letter: Q
Glutamine
47
3-letter: Ser
Serine
48
1-letterL S
Serine
49
3-letter: Thr
Threonine
50
1-letter: T
Threonine
51
Which amino acid residues can be oxidized to form a disulfide bond?
Cysteine
52
Which Amino Acid contains a sulfhydryl group?
Cysteine
53
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?
Disulfide bond
54
What is a nucleophile?
Reactant that provides a pair of electrons to form a new covalent bond
55
Name the 2 roles of Cysteine in proteins
(1) Enhance protein stability through disulfide bonds | (2) Important in catalytic functions of many enzymes, as the deprotonated -SH is a good nucleophile
56
Which amino acids' side chains contain an amide group that can act as both a donor or acceptor of electrons? (2)
Asparagine & Glutamine
57
Describe the side Chains of Asparagine and Glutamine (2)
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
Describe the side chains of Serine and Threonine (2)
They have an hydroxyl group capable of forming hydrogen bonds. They can also be phosphorylated by kinases, resulting in protein modifications.
59
Polar negatively charged Amino Acids (2)
Apartate, Glutamate
60
3-letter: Asp
Aspartate
61
1-letter: D
Aspartate
62
3-letter: Glu
Glutamate
63
1-letter: E
Glutamate
64
Describe the side chains of aspartate and glutamate
Contains a carboxyl group and therefore carry a negative charge at pH 7.0
65
What are the 3 polar, positively charged amino acids?
Lysine, Arginine, Histidine
66
3-letter: Lys
Lysine
67
1-Letter: K
Lysine
68
3-letter: Arg
Arginine
69
1-letter: R
Arginine
70
3-letter: His
Histidine
71
1-letter: H
Histidine
72
Which amino acid contains a side chain amino group?
Lysine
73
Which amino acid contains a side chain guanidinium group?
Arginine
74
Which Amino acids contains an imidazole group?
Histidine
75
Where do charged amino acids tend to be located?
The exterior of proteins, in contact with water, because they are very hydrophilic and able to make hydrogen bonds with water
76
Why are charged amino acids important to enzyme function?
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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