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BIOCHEMISTRY > MODULE 1A.1: Amino Acids and Proteins > Flashcards

MODULE 1A.1: Amino Acids and Proteins Flashcards

1
Q

What are the structural components of an amino acid?

A

1) Central carbon (α-carbon)
2) Amino group
3) Carboxyl group
4) Side chain (R group)

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2
Q

What is the difference between L and D amino acids?

A

1) L = Levo = Left
2) D = Dextro = Right

These are based on the position of the amino group.

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3
Q

In the human body, amino acids exist as ___________.

A

L-α-amino acids

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4
Q

How many amino acids are translated in the human genome?

A

20

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5
Q

Enumerate the amino acids with aliphatic side chains. [5]

A

1) Glycine
2) Alanine
3) Valine
4) Leucine
5) Isoleucine

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6
Q

Which of the amino acids with aliphatic side chains are linear? [3]

A

1) Glycine
2) Alanine
3) Valine

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7
Q

Which of the amino acids with aliphatic side chains are branched? [2]

A

1) Leucine

2) Isoleucine

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8
Q

Enumerate the amino acids with side chains containing hydroxyl (-OH) groups. [3]

A

1) Serine
2) Threonine
3) Tyrosine

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9
Q

What does the hydroxyl group contribute to the amino acid’s function? [1]

A

Allow proteins to interact with other proteins, usually via hydrogen bonding

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10
Q

Enumerate the amino acids with side chains containing sulfur (-SH) groups. [2]

A

1) Cysteine

2) Methionine

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11
Q

What does the sulfur group contribute to the amino acid’s function? [2]

A

1) Allow proteins to interact with other proteins

2) Catalytic process of enzymes

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12
Q

Enumerate the amino acids with side chains containing acidic groups and their amides. [4]

A

1) Aspartic Acid or Aspartate
2) Asparagine
3) Glutamic Acid or Glutamate
4) Glutamine

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13
Q

What is the difference between aspartate and asparagine or glutamate and glutamine?

A

There is an extra amino (-NH2) group in asparagine and glutamine

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14
Q

Enumerate the amino acids with side chains containing basic groups. [3]

A

1) Arginine
2) Lysine
3) Histidine

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15
Q

Which functional group is responsible for the basicity of arginine, lysine, and histidine?

A

Amine Groups

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16
Q

Enumerate the amino acids with side chains containing aromatic rings. [4]

A

1) Phenylalanine
2) Tryptophan
3) Tyrosine
4) Histidine

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17
Q

TRUE OR FALSE?

Structurally, proline is NOT an amino acid.

A

TRUE. It is an imino acid.

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18
Q

Amino acid that is classified as an imino acid.

A

Proline

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19
Q

What are the characteristics of amino acids that are non-polar? [2]

A

1) Neutral charge

2) Hydrophobic

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20
Q

TRUE OR FALSE?

Polar amino acids are ALWAYS positively charged.

A

FALSE. Some polar amino acids are uncharged or neutral.

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21
Q

What are the two classifications of polar and charged amino acids?

A

1) Acidic

2) Basic

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22
Q

Complete the following:

acidic amino acids : __________ charged :: basic amino acids : __________ charged

A

acidic amino acids : negatively charged :: basic amino acids : positively charged

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23
Q

Which functional groups are responsible for polar amino acids?

A

Hydroxyl (-OH) and sulfur (-SH) groups

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24
Q

What is the smallest amino acid? What does this do for its function?

A

Glycine; It’s small size allows it to fit in regions that are inaccessible to other amino acids

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25
Q

What group of amino acids are hydrophobic? How does this affect protein folding?

A

Aliphatic and aromatic groups; Proteins will fold in such a way where these amino acids will be found in the interior

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26
Q

Where are the charged amino acids located in protein folding?

A

Exterior of the protein

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27
Q

What is the function of charged amino acids in protein conformation?

A

Stabilization with ionic bonds or salts

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28
Q

What is the function of amino acids containing hydroxyl side chains? Where are they usually found?

A

Signaling; Exterior of the protein

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29
Q

What group is unique to histidine?

A

Imidazole group

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30
Q

What are the functions of the imidazole group of histidine?

A

1) Important in enzyme catalysis

2) Buffer for acid-base balance at physiologic pH

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31
Q

Which amino acid is structurally similar to the 21st amino acid?

A

Cysteine

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32
Q

Where is selenocysteine derived from?

A

Serine

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33
Q

What structure is different between cysteine and selenocysteine?

A

Sulfur residue of cysteine is replaced with selenium for selenocysteine

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34
Q

Identify the enzymes that utilize selenocysteine and their functions.

A

1) Thioredoxin - DNA regulation
2) Glutathione peroxidase - Anti-oxidant properties
3) Deiodinase -Activation of thyroid hormones

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35
Q

What is the disease associated with selenocysteine deficiency?

A

Keshan Disease

36
Q

What is Keshan disease and how does it occur?

A

Dilated cardiomyopathy or heart failure caused by excessive oxidative stress. It occurs because glutathione peroxidase cannot be produced due to selenocysteine deficieny.

37
Q

Amino acid where thyroid hormones are derived from.

A

Tyrosine

38
Q

Amino acid where serotonin and melatonin are derived from.

A

Tryptophan

39
Q

What are the functions of hormones derived from tryptophan? [3]

A

Serotonin and Melatonin: Mood, sleep and cognitive function

40
Q

Amino acid where dopamine, norepinephrine, and epinephrine are derived from.

A

Tyrosine

41
Q

What are the functions of hormones derived from tyrosine? [3]

A

Dopamine and Norepinephrine: Attention and motivation

Epinephrine: Sympathetic nervous system

42
Q

Amino acid where histamine is derived from.

A

Histidine

43
Q

What is the function of the hormone derived from histidine?

A

Histamine: Inflammation

44
Q

Amino acid where nitric oxide is derived from.

A

Arginine

45
Q

What is the function of the hormone derived from arginine?

A

Nitric Oxide: Vasodilation

46
Q

Amino acid where carnitine is derived from.

A

Lysine

47
Q

What is the function of the hormone derived from lysine?

A

Carnitine: Fat metabolism

48
Q

What links amino acids together?

A

Peptide bonds

49
Q

TRUE OR FALSE?

Peptide bonds possess a double-bond character.

A

FALSE. Peptide bonds have a PARTIAL double-bond character.

50
Q

What do you call a peptide with less than or equal to twenty amino acids?

A

Oligopeptide

51
Q

What do you call a peptide with more than twenty amino acids?

A

Polypeptide

52
Q

What is the process of peptide bond formation?

A

Condensation

53
Q

TRUE OR FALSE?

Peptide bond formation involves the addition of water to condense the amino acids involved.

A

FALSE. It involves the REMOVAL of water.

54
Q

An important peptide that is well-known for its anti-oxidant properties.

A

Glutathione

55
Q

What is the amino acid composition of glutathione?

A

Glutamyl-Cysteinyl-Glycine (Glutamate, Cysteine, and Glycine)

56
Q

Glutathione participates in the formation of correct disulfide bonds of many proteins. What amino acid and functional group is responsible for this?

A

Cysteine; Sulfur (-SH) group.

57
Q

What is the amino acid composition of thyrotropin?

A

Pyroglutamyl-histidyl-prolinamide

58
Q

Where is thyrotropin produced?

A

Hypothalamus

59
Q

What is the function of thyrotropin?

A

Controls the pituitary gland’s regulation of the thyroid-stimulating hormone

60
Q

Synthetic peptide that is used as an artificial sweetener

A

Aspartame

61
Q

What is the composition of aspartame?

A

Aspartic acid, Phenylalanine, and Methanol

62
Q

Describes the sequence of amino acids.

A

Primary structure

63
Q

What are the classes of secondary proteins?

A

1) Globular

2) Fibrous

64
Q

What globular protein is most abundant in blood?

A

Haemoglobin

65
Q

What is the most abundant measurable protein in the plasma?

A

Albumin

66
Q

What fibrous protein is most abundant in tissues or organs?

A

Collagen

67
Q

This is the most secondary structure in globular proteins.

A

Alpha helices

68
Q

What stabilizes the alpha helix?

A

Hydrogen bonding between two non-adjacent amino acids

69
Q

What is the most likely reason for a kink or broken hydrogen bond in an alpha helix?

A

Presence of proline

70
Q

How do charged amino acids disrupt the alpha helix?

A

1) Formation of ionic bonds

2) Exerts electrostatic forces which repel each other

71
Q

What stabilizes beta sheets?

A

Hydrogen bonding

72
Q

What stabilizes beta sheets?

A

Hydrogen bonding

73
Q

Enumerate the forces that govern the protein folding in tertiary structures. [5]

A

1) Hydrogen bonds
2) Hydrophobic interactions
3) Disulfide bonds
4) Electrostatic interactions or salt bridges
5) van der Waals forces

74
Q

Present in proteins composed of two or more polypeptide chains

A

Quarternary structure

75
Q

You found out that your patient suffers from Vitamin C deficiency. How does this affect collagen?

A

Quality of collagen decreases because Vitamin C maintains the hydrogen bonding in the polypeptide chain

76
Q

What structure do mutations primarily affect?

A

Primary structure

77
Q

What type of mutation occurs in sickle cell anemia?

A

Missense Mutation

78
Q

What macromolecule are the three complex protein structures associated with?

A

1) Glycoprotein - carbohydrates
2) Proteoglycans - polysaccharides
3) Lipoproteins - lipids

79
Q

What type of bonding is present between the protein and carbohydrates of glycoproteins?

A

Covalent bonding

80
Q

What are the two classes of glycoproteins?

A

1) N-linked

2) O-linked

81
Q

What is characteristic of N-linked sugars?

A

Carbohydrate is attached to the amide of asparagine.

82
Q

What is characteristic of O-linked sugars?

A

Carbohydrate is attached to the hydroxyl groups of serine, threonine, or hydroxylysine

83
Q

What complex protein structure defines blood types?

A

Glycoproteins

84
Q

Where are proteoglycans abundant?

A

Connective tissue

85
Q

Transports lipid molecules in the blood

A

Lipoproteins

86
Q

Responsible for docking onto receptors to unload lipoprotein content

A

Apolipoproteins

BIOCHEMISTRY (2 decks)

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