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BioChemistry Exam 1 > Biochemistry Chapter 3 AA, peptides and proteins. > Flashcards

Biochemistry Chapter 3 AA, peptides and proteins. Flashcards

1
Q

What are some functions of proteins?

A

•Mediate every process in a cell.

i. Enzymes
ii. Hormones
iii. Antibodies
iv. Transports
v. Muscle fibers
vi. Lens of the eye
vii. Buffers.

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2
Q

Which AA does not have a chiral center?

A

•All amino acids, except GLYCINE have chiral Centers.

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3
Q

define Nonpolar

A

does not like polar compounds

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4
Q

define Aliphatic

A

Contains a hydrocarbon

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5
Q

does not like polar compounds

A

Nonpolar

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6
Q

Contains a hydrocarbon

A

Aliphatic

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7
Q

D amino Acids

A

CORN Counterclockwise

Fit in taste butts

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8
Q

L Amino acids

A

CORN Clockwise
Found in nature
Can’t fit into taste buds

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9
Q

Which AA are metabolized in muscle?

A

Leucine, Isoleucine, Valine

Glutamate, Aspartate, Asparagine (GAA)

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10
Q

Important for muscle synthesis.

A

Leucine, Isoleucine, Valine

Glutamate, Aspartate, Asparagine (GAA)

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11
Q

Leucine, Isoleucine, Valine

Glutamate, Aspartate, Asparagine (GAA)

A

metabolized in muscle

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12
Q

Leucine

A

Essential non polar (branch Chain)

metabolized into cholesterol

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13
Q

metabolized in muscle

A

Leucine, Isoleucine, Valine

Glutamate, Aspartate, Asparagine (GAA)

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14
Q

Isoleucine

A

structural isomer of leucine

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15
Q

structural isomer of leucine

A

Isoleucine

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16
Q

Where are the remaining AA metabolized at?

A

Liver

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17
Q

• Genetic deficiency on enzyme- required to metabolize branched chain amino acids (Valine Leucine, Isoleucine)—L.I.V

A

Maple Syrup Urine Disease

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18
Q

Symptoms Urine with color, odor and viscosity of maple syrup

A

Maple Syrup Urine Disease

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19
Q

If untreated, it can cause brain damage and death

A

Maple Syrup Urine Disease

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20
Q

Treatment: AVOID high protein food for life.

A

Maple Syrup Urine Disease

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21
Q

•Its an autoimmune condition- IgA related

A

Celiac Disease

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22
Q

•Genetic Susceptibility – exposure to gluten -> Environmental triggers - Autoimmune response.

A

Celiac Disease

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23
Q

Genetic disorder that lacks Enzyme necessary to metabolize phenylalanine.

A

Phenylketonuria (PKU)

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24
Q

Causes brain damage

A

D. Phenylketonuria (PKU)

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25
Q

Phenylalanine Found in NutraSweet and anything with protein.

A

D. Phenylketonuria (PKU)

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26
Q

Treatment: Avoid phenylalanine in diet (low protein)

A

D. Phenylketonuria (PKU)

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27
Q

Genetic mutation that occurred over time to protect population from malaria but is Very Painful.

A

Sickle cell Anemia

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28
Q

• Valine (nonpolar) replaces glutamate (polar) in hemoglobin
o Causing it to fold incorrectly.

A

Sickle cell Anemia

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29
Q

Sickle cell Anemia

A

Globular proteins–> Highly folded  Defected in Folding-Accumulate leading to sickle cell anemia. (Where its folded incorrectly but the body accumulates it there a reason for it.)

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30
Q

used to make glucose, if necessary (product= Pyruvate)

A

Glucogenic

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31
Q

turned into Krebs cycle intermediate ketone bodies to fatty acids, if in excess (product= acetyl CoA)

A

Ketogenic

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32
Q

Glucogenic

A

used to make glucose, if necessary (product= Pyruvate)

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33
Q

Ketogenic

A

turned into Krebs cycle intermediate ketone bodies to fatty acids, if in excess (product= acetyl CoA)

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34
Q

Uncommon Amino Acids (found in collagen)

A

Hydroxyproline

Hydroxylysine

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35
Q

Uncommon Amino Acids (part of myosin)

A

Methyllysine

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36
Q

Uncommon Amino Acids (part of elastin)

A

Desmosine

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37
Q

Hydroxyproline

Hydroxylysine

A

Uncommon Amino Acids (found in collagen)

38
Q

Methyllysine

A

Uncommon Amino Acids (part of myosin)

39
Q

Desmosome

A

Uncommon Amino Acids (part of elastin)

40
Q

Found in proteins that stimulate clotting and bone synthesis.

A

Carboxyglutamate

41
Q

o A glutamate A.A with extra carboxylic acid.

A

Carboxyglutamate

42
Q

Special A.A derivative that uses selenium instead of sulfur

A

Selenocysteine

43
Q

Essential AA (branch chains)

A

Valine
Isoleucine
Leucine

44
Q

Essential AA (base )

A

Histidine

Lysine

45
Q

Presucurser for Histidine

A

Histamine

46
Q

Presucurser for Lysine

A

Collagen

47
Q

Presucurser for Leucine

A

Cholesterol

48
Q

Presucurser for Methionine

A

SAMe

49
Q

Essential AA (all of them)

A 
Phenylalanine
Valine 
Methionine 
Threonine 
Histidine Histamine 
Isoleucine 
 Lysine 
 Leucine
50
Q

derivates of Methionine

A

SAMe, sulfur containing precursor for S-adenosyl methionine ( needed for myelination)

51
Q

derivates Proline

A

Collagen, Disrupts -α- helix and β-helix pleated sheet (secondary Structure) (Collagen loves it)

52
Q

derivates Tyrosine

A

Thyroid hormones, melanin and catecholamines (dopamine, epinephrine and norepinephrine); Cell signaling.

53
Q

derivates Serine

A

H-bonding

54
Q

H-bonding

A

Serine

55
Q

derivates Glutamic acids

A

GABA

56
Q

GABA

A

Glutamic acids

57
Q

derivates • Glutamine

A

Main N carrier

58
Q

Derivates • Cysteine

A

Disulfide

59
Q

Derivates • Tryptophan

A

melatonin, serotonin and niacin.

60
Q

melatonin, serotonin and niacin.

A

Tryptophan

61
Q

Main N carrier

A

Glutamine

62
Q

Disulfide

A

Cysteine

63
Q

Amphoteric

A

All have at least 2 charges at physiologic pH 

64
Q

pH ↓ [H] ↑= AA can act as Bases

A

Proton acceptor

65
Q

pH ↑ [H] ↓= AA can act as Acids

A

Proton Donor

66
Q

Proton acceptor

A

pH ↓ [H] ↑= AA can act as Bases

67
Q

Proton Donor

A

pH ↑ [H] ↓= AA can act as Acids

68
Q

pH below pK

A

H is still attached-Pronated

69
Q

pH above pK

A

H is lost deprotonated

70
Q

Pronated

A

H is still attached

pH below pK

71
Q

deprotonated

A

H is lost

pH above pK

72
Q

pK1:

A

: removal of H from carboxyl group

73
Q

pK2:

A

: removal of H from amino group

74
Q

pKR:

A

Removal of H from R group

75
Q

: removal of H from carboxyl group

A

pK1:

76
Q

: removal of H from amino group

A

pK2:

77
Q

Removal of H from R group

A

pKR:

78
Q

What is a zwitterion is it good buffer at this point ?

A

The point where an amino acids or protein is neutral

It not a good buffer at this point.

79
Q

The point where an amino acids or protein is neutral

A

zwitterion

80
Q

What does protonated

A

Pronated: H is attached

81
Q

What does deprotonated mean?

A

Depronated: H is not attached.

82
Q

How are peptide bonds formed?

A

• Dehydration run between N- terminal and of one AA and the C terminal of another AA

83
Q

Chains of amino Acids

A

Peptides

84
Q

Chains of amino Acids molecular weight>10,000

A

Proteins

85
Q

Contains peptide bond formed by dehydration

A

Peptides

86
Q

Contains peptide bonds

A

Proteins

87
Q

Many amino acids is called polypeptide.

A

Peptides

88
Q

Name the prosthetic group of lipoprotein, and give me an example?

A

Lipids

Example :VLDL

89
Q

Name the prosthetic group of Glycoprotein,and give me an example?

A

Carbohydrates

example: Immunoglobulin G

90
Q

Name the prosthetic group Phosphoproteins, and give me an example?

A

Phosphates

example : Casein in milk

91
Q

Name the prosthetic group Hemeproteins , and give me an example ?

A

Heme (protoporphyrin)

example: Hemoglobin

92
Q

Name the prosthetic group Metalloproteins, and give me an example ?

A

Iron, zinc, calcium

Example : Ferritin, alcohol dehydration calmodulin.

BioChemistry Exam 1 (5 decks)

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