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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
What group of amino acids are hydrophobic? How does this affect protein folding?
Aliphatic and aromatic groups; Proteins will fold in such a way where these amino acids will be found in the interior
26
Where are the charged amino acids located in protein folding?
Exterior of the protein
27
What is the function of charged amino acids in protein conformation?
Stabilization with ionic bonds or salts
28
What is the function of amino acids containing hydroxyl side chains? Where are they usually found?
Signaling; Exterior of the protein
29
What group is unique to histidine?
Imidazole group
30
What are the functions of the imidazole group of histidine?
1) Important in enzyme catalysis | 2) Buffer for acid-base balance at physiologic pH
31
Which amino acid is structurally similar to the 21st amino acid?
Cysteine
32
Where is selenocysteine derived from?
Serine
33
What structure is different between cysteine and selenocysteine?
Sulfur residue of cysteine is replaced with selenium for selenocysteine
34
Identify the enzymes that utilize selenocysteine and their functions.
1) Thioredoxin - DNA regulation 2) Glutathione peroxidase - Anti-oxidant properties 3) Deiodinase -Activation of thyroid hormones
35
What is the disease associated with selenocysteine deficiency?
Keshan Disease
36
What is Keshan disease and how does it occur?
Dilated cardiomyopathy or heart failure caused by excessive oxidative stress. It occurs because glutathione peroxidase cannot be produced due to selenocysteine deficieny.
37
Amino acid where thyroid hormones are derived from.
Tyrosine
38
Amino acid where serotonin and melatonin are derived from.
Tryptophan
39
What are the functions of hormones derived from tryptophan? [3]
Serotonin and Melatonin: Mood, sleep and cognitive function
40
Amino acid where dopamine, norepinephrine, and epinephrine are derived from.
Tyrosine
41
What are the functions of hormones derived from tyrosine? [3]
Dopamine and Norepinephrine: Attention and motivation | Epinephrine: Sympathetic nervous system
42
Amino acid where histamine is derived from.
Histidine
43
What is the function of the hormone derived from histidine?
Histamine: Inflammation
44
Amino acid where nitric oxide is derived from.
Arginine
45
What is the function of the hormone derived from arginine?
Nitric Oxide: Vasodilation
46
Amino acid where carnitine is derived from.
Lysine
47
What is the function of the hormone derived from lysine?
Carnitine: Fat metabolism
48
What links amino acids together?
Peptide bonds
49
TRUE OR FALSE? Peptide bonds possess a double-bond character.
FALSE. Peptide bonds have a PARTIAL double-bond character.
50
What do you call a peptide with less than or equal to twenty amino acids?
Oligopeptide
51
What do you call a peptide with more than twenty amino acids?
Polypeptide
52
What is the process of peptide bond formation?
Condensation
53
TRUE OR FALSE? Peptide bond formation involves the addition of water to condense the amino acids involved.
FALSE. It involves the REMOVAL of water.
54
An important peptide that is well-known for its anti-oxidant properties.
Glutathione
55
What is the amino acid composition of glutathione?
Glutamyl-Cysteinyl-Glycine (Glutamate, Cysteine, and Glycine)
56
Glutathione participates in the formation of correct disulfide bonds of many proteins. What amino acid and functional group is responsible for this?
Cysteine; Sulfur (-SH) group.
57
What is the amino acid composition of thyrotropin?
Pyroglutamyl-histidyl-prolinamide
58
Where is thyrotropin produced?
Hypothalamus
59
What is the function of thyrotropin?
Controls the pituitary gland's regulation of the thyroid-stimulating hormone
60
Synthetic peptide that is used as an artificial sweetener
Aspartame
61
What is the composition of aspartame?
Aspartic acid, Phenylalanine, and Methanol
62
Describes the sequence of amino acids.
Primary structure
63
What are the classes of secondary proteins?
1) Globular | 2) Fibrous
64
What globular protein is most abundant in blood?
Haemoglobin
65
What is the most abundant measurable protein in the plasma?
Albumin
66
What fibrous protein is most abundant in tissues or organs?
Collagen
67
This is the most secondary structure in globular proteins.
Alpha helices
68
What stabilizes the alpha helix?
Hydrogen bonding between two non-adjacent amino acids
69
What is the most likely reason for a kink or broken hydrogen bond in an alpha helix?
Presence of proline
70
How do charged amino acids disrupt the alpha helix?
1) Formation of ionic bonds | 2) Exerts electrostatic forces which repel each other
71
What stabilizes beta sheets?
Hydrogen bonding
72
What stabilizes beta sheets?
Hydrogen bonding
73
Enumerate the forces that govern the protein folding in tertiary structures. [5]
1) Hydrogen bonds 2) Hydrophobic interactions 3) Disulfide bonds 4) Electrostatic interactions or salt bridges 5) van der Waals forces
74
Present in proteins composed of two or more polypeptide chains
Quarternary structure
75
You found out that your patient suffers from Vitamin C deficiency. How does this affect collagen?
Quality of collagen decreases because Vitamin C maintains the hydrogen bonding in the polypeptide chain
76
What structure do mutations primarily affect?
Primary structure
77
What type of mutation occurs in sickle cell anemia?
Missense Mutation
78
What macromolecule are the three complex protein structures associated with?
1) Glycoprotein - carbohydrates 2) Proteoglycans - polysaccharides 3) Lipoproteins - lipids
79
What type of bonding is present between the protein and carbohydrates of glycoproteins?
Covalent bonding
80
What are the two classes of glycoproteins?
1) N-linked | 2) O-linked
81
What is characteristic of N-linked sugars?
Carbohydrate is attached to the amide of asparagine.
82
What is characteristic of O-linked sugars?
Carbohydrate is attached to the hydroxyl groups of serine, threonine, or hydroxylysine
83
What complex protein structure defines blood types?
Glycoproteins
84
Where are proteoglycans abundant?
Connective tissue
85
Transports lipid molecules in the blood
Lipoproteins
86
Responsible for docking onto receptors to unload lipoprotein content
Apolipoproteins

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