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Biochemistry > Module 01: Amino Acids > Flashcards

Module 01: Amino Acids Flashcards

1
Q

These are the building blocks of proteins. And all have the same basic structure.

A

Amino acids

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2
Q

What comprises an amino acid?

A

(1) Amino group
(2) Carboxyl group
(3) Alpha H
(4) Side Chain (R)

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3
Q

This gives identity to amino acid.

A

R group

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4
Q

There are two (2) stereoisomers:

A

L and D

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5
Q

Where is the amino acid in D-stereoisomers?

A

Right

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6
Q

Where is the amino acid in L-stereoisomers?

A

Left

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7
Q

These are characterized to be non super imposable and pertains to two amino acids that are not the same but hold mirror-like images.

A

Enantiomers

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8
Q

if the side chain is hydrogen, it is called “_________________”.

A

Glycine

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9
Q

if the side chain is methyl (CH3), it is called “_________________”.

A

Alanine

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10
Q

The amino group and the carboxyl group are bonded to the same carbon atom called “__________________.”

A

Alpha Carbon Atom

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11
Q

How many alpha amino acids are encoded by the genetic code share the generic structure?

A

20

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12
Q

When carbon has four different groups attached to it, it is called “_____________” or “_________________”

A

Chiral or Asymmetric

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13
Q

This is cyclic amino acid, is the exception to the basic structure of amino acids.

A

Proline

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14
Q

Where are L isomers found?

A

Proteins

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15
Q

Where are D isomers found?

A

Cell wall of bacteria and peptide antibiotics

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16
Q

This pertains to amino acids with side chains that do not like to reside in an aqueous environment; hence, prompting them to reside in the core of the protein.

A

Hydrophobic

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17
Q

This is a hydrophobic group that contains only carbon or hydrogen atoms.

A

Aliphatic

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18
Q

This is the simplest amino acid, although placed under nonpolar and aliphatic its small H do not contribute much to hydrophobic interactions.

A

Glycine

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19
Q

These amino acids are those with side-chains that prefer to reside in an aqueous environment and hence can be generally found exposed on the surface of a protein.

A

Polar amino acids

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20
Q

what is the ph of non-polar, aliphatic groups?

A

7

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21
Q

What are the types of nonpolar aliphatic r groups? (GAVILM)

A

(1) Glycine
(2) Alanine
(3) Proline
(4) Valine
(5) Isoleucine
(6) Leucine
(7) Methionine

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22
Q

What are the types of Aromatic r groups? (PTT)

A

(1) Phenylalanine
(2) Tyrosine
(3) Tryptophan

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23
Q

What is the side chain of phenylalanine?

A

Benzene Ring (nonpolar)

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24
Q

What is the side chain of tyrosine?

A

Phenolic OH group (polar and ionizable, has pK3

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25
Q

What is the side chain Tryptophan?

A

Indole Ring

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26
Q

What are the types of Polar, uncharged r groups? (STACG)

A

(1) Serine
(2) Threonine
(3) Cysteine
(4) Asparagine
(5) Glutamine

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27
Q

The side chains do not ionize at pH 7 but are capable of hydrogen bonding with water.

A

Polar, uncharged r groups

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28
Q

These polar, uncharged r groups contain the polar hydroxyl group.

A

(1) Serine
(2) Threonine

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29
Q

This polar, uncharged r groups contains thiol/sulfhydryl group

A

Cysteine

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30
Q

What are the types of positively charged r groups? (LAH)

A

(1) Lysine
(2) Arginine
(3) Histidine

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31
Q

What amino group does lysine contain?

A

epsilon

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32
Q

What amino group does arginine contain?

A

guanidino

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33
Q

These can display ionic interactions with basic AA (+) or H – bond with OH containing amino acids

A

Negatively Charged r groups

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34
Q

What are the types of negatively charged r groups?

A

(1) Aspartate
(2) Glutamate

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35
Q

This is a fibrous protein of connective tissues.

A

Collagen

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36
Q

These are found mainly in collagen and gelatin proteins.

A

Hydroxyproline and Hydroxylysine

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37
Q

This is iodinated AA found only in thyroglobulin in the thyroid gland.

A

Thyroxine

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38
Q

This Is found in proteins involved in blood clotting.

A

y-carboxyglutamic acid

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39
Q

These are residues created by modification of AA residues already incorporated into a polypeptide

A

Uncommon Amino acids

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40
Q

This is an important chemical messenger involved in reward, motivation, memory, attention and even regulating body movements.

A

Dopamine

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41
Q

It is the inactive form and most of it is converted to an active form called _______________by organs such as the liver and kidneys.

A

triiodothyronine

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42
Q

This is a neurotransmitter or chemical messenger in the brains that blocks specific signals in the central nervous system; thus slowing down the brain and providing protective or calming effect.

A

Gamma-aminobutyric acid

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43
Q

This pertains to the oxidation of 2 cysteine to form cystine (Cys). These are used to stabilize the structures of many proteins.

A

Disulfide Bond Formation

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44
Q

This is used to convert pro and lys to OH-pro and OH-lys

A

Hydroxylation

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45
Q

This is synthesized by decarboxylation of histidine

A

Histamine

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46
Q

This is derived from tryptophan, that similarly functions as neurotransmitters and regulators.

A

Serotonin

47
Q

This is found in nature in the peptides carnosine and anserine and is a component of pantothenic acid (vitamin a).

A

B-alanine

48
Q

This is derived from tyrosine.

A

Epinephrine (Adrenaline)

49
Q

This is a constituent of the penicillin antibiotics.

A

Penicillamine

50
Q

These are known to be important metabolic intermediates (BOHOMOHOMO)

A

(1) Betaine
(2) Ornithine
(2) Homocysteine
(4) Homoserine

51
Q

This is a derivative of 4 lysine residues found in the fibrous protein elastin.(con tissue prot)

A

Desmosine

52
Q

This is a rare amino acid derived from serine. It is introduced during protein synthesis and not a product of modification. It contains selenium and not sulfur

A

Selenocysteine

53
Q

These are two amino acids not found in proteins, are intermediates in the biosynthesis of arginine and in the urea cycle

A

Ornithine and citrulline

54
Q

This is produced by the pineal gland, a small endocrine gland found outside of the BBB. This is a part of a system that regulates sleep and wake cycle by chemically causing drowsiness and lowering the body.

A

Melatonin

55
Q

What are the functions of amino acids?

A

(1) Components of proteins
(2) Formation of glucose (glucogenic AA)
(3) Precursors of nitrogen containing compounds
(4) Transport and storage form of ammonia (glN)
(5) Buffer
(6) Chemical messengers/neurotransmitters
(7) Detoxification reactions

56
Q

These are neurotransmitters derived from tyrosine. Include dopamine, epinephrine and norepinephrine.

A

Catecholamines

57
Q

Where is gamma-aminobutyric derived from?

A

Glutamate

58
Q

What are the essential amino acids?

A

(1) Arginine
(2) Histidine
(3) Isoleucine
(4) Leucine
(5) Lysine
(6) Methionine
(7) Phenylalanine
(8) Threonine
(9) Tryptophan
(10) Valine

Ako, Heto si Isko LaLab mo, PaTay na paTay kay Vicky

59
Q

What are the non-essential amino acids?

A

(1) Alanine
(2) Asparagine
(3) Aspartate
(4) Cysteine
(5) Glutamate
(6) Glutamine
(7) Glycine
(8) Proline
(9) Serine
(10) Tyrosine

60
Q

This is known as a potent vasodilator released as part of the immune response. Moreover, this increases localized blood volume for white blood cells

A

Histamine

61
Q

This includes a description of all covalent bonds (peptide and disulfide bonds) linking amino acids in the polypeptide chain.

A

Primary Structure

62
Q

This refers to the sequence of amino acid residues from the N –terminal to the C- terminal. This determines how a protein folds into a unique 3-d structure.

A

Primary Structure

63
Q

This refers to stable arrangements of AA residues giving rise to recurring structural patterns.

A

Secondary structure

64
Q

This describes all aspects of 3- dimensional folding of a polypeptide

A

Tertiary structure

65
Q

This describes the arrangement in space of a protein consisting of 2 or more subunits.

A

Quaternary structure

66
Q

This is the sequence of amino acids in a polypeptide chain, read from the N-terminal end to the C-terminal end

A

Primary Structure

67
Q

This pertains to the ordered 3-dimensional arrangements (conformations) in localized regions of a polypeptide chain; refers only to interactions of the peptide backbone

A

Secondary structure

68
Q

This is the arrangement of monomer subunits with respect to each other

A

Quaternary structure

69
Q

This refers to spatial arrangement of amino acids that are adjacent in a segment of a polypeptide chains, They do not consider the side chains

A

Secondary structure

70
Q

How many amino acids are generated per turn in an alpha helix?

A

3.6 (5.4)

71
Q

Side chains of AA residues ________________from the helical backbone.

A

Protrude outwards

72
Q

The hydrogen-bonds are ___________to the helical axis

A

Parallel

73
Q

Alpha Helixes are stabilized by what?

A

Stabilized by H-bond between NH and C=O of the peptide bonds. All peptide bond components participate in H- bonding.

74
Q

Alpha helixes are destabilized by what?

A

Proline (helix breaker) and glycine (which tends to form coiled structures different from an a-helix)

75
Q

In this, the polypeptide backbone is tightly wound around an imaginary axis

A

Alpha helix

76
Q

Which alpha helix is more stable, right or left?

A

Right alpha helix

77
Q

These organizes polypeptides into sheets. An extended zigzag conformation of protein backbones. In this, the protein backbones are arranged side-by-side through H-bonds.

A

B-pleated sheet

78
Q

In beta pleated sheets, h-bonds are _____________to the backbone direction

A

perpendicular

79
Q

In beta pleated sheets, the side chains of adjacent AAs protrude in _____________.

A

opposite directions (parallel or anti-parallel)

80
Q

These are like silk fibroin and fibroin of spider webs

A

B-keratin

81
Q

These beta pleated sheets run in an opposite direction of its neighbor (A)

A

Anti-parallel

82
Q

These beta pleated sheets run in the same direction with longer looping sections between them (B)

A

Parallel

83
Q

These beta sheets reverses the direction of a polypeptide chain and connect the ends of two adjacent segments of antiparallel - sheet.

A

Beta Turns

84
Q

How are beta turns generated?

A

The structure is a 180o turn involving four amino acid residues, where the carbonyl group of the first residue forms an H –bond with the amino group of the fourth

85
Q

These residues often occur in b-turns

A

Glycine and Proline

86
Q

This type of beta turns usually involves proline as the 2nd amino acid residue

A

Type I

87
Q

This type of beta turns usually have glycine as the 3rd residue

A

Type II

88
Q

This three dimensional globular structure formed by bending and twisting of the polypeptide chain. This is also known as the highest order for monomeric protein

A

Tertiary Structure

89
Q

What are the interactions included for tertiary structures?

A

(1) Hydrophobic interactions  hydrophobic amino acid side chains into the interior of the protein shielding them from water
(2) Disulfide bonds
(3) Hydrogen bonds
(4) Electrostatic interactions between charged amino acid side chains

90
Q

This structure is known as the association of the polypeptide chains

A

Quaternary Structure

91
Q

In the quaternary structure, each polypeptide chain in the protein is called ________________.

A

Subunit (homo or hetero)

92
Q

This is a pancreatic hormone consisting of 2 polypeptide chains

A

Insulin

93
Q

This is a pancreatic hormone that opposes insulin

A

Glucagon

94
Q

This is a local hormone produced by the stomach, stimulates the secretion of gastric juice

A

Gastrin

95
Q

This is a a tripeptide of glutamate, cysteine and glycine, it is found in all mammalian cells except neurons.

A

Glutathione

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Q
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Biochemistry (16 decks)

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