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Biochem > problem set 8 > Flashcards

problem set 8 Flashcards

LACKS conversion between IE and pH changes

1
Q

NO chiral carbons

A

glycine

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2
Q

Two chiral carbons

A

isoleucine

threonine

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3
Q

at a pH of 9.7 alaine

A

-1

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4
Q

at a pH of 9.7 glutamic acid

A

-2

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5
Q

at a pH of 9.7

lysine

A

0

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6
Q

at a pH of 9.7
alanine, glutamic acid, lysine
-positive electrode-

A

move to the positive electrode

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7
Q

at a pH of 9.7
alanine, glutamic acid, lysine
-negative electrode-

A

none

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8
Q

at a pH of 9.7
alanine, glutamic acid, lysine
-don’t move-

A

lysine

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9
Q

pH 9 the protein would have a ____

A

negative charge

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10
Q

pH 4 it would have __

A

positive charge

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11
Q

proteins are least soluble

A

at their isoelectric point

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12
Q

when the isoelectric points are negative

A

they move to the positive electrode

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13
Q

changes in the pH most affect what type of bonding in proteins

A

ionic interactions (salt bridges)

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14
Q

polypeptides with few acid or basic side chain amino acids are less sensitive to pH changes than polypeptides with a higher number of side chains

A

the acid and basic side chains are in the salt bridge
polypeptides with few acid and basic side chains have very few salt bridges
thus they are not sensitive to pH change

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15
Q

what type of bonding is found in the primary structure of proteins

A

amide bond

amide bond is the same as a peptide linkage

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16
Q

what type of bonding is NOT found between protein chains in the quaternary structure

A

hydrophobic interactions

hydrophobic amino acid side chains are mostly found in the inside of a globular protein

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17
Q

hydrogen bonding of “O” in the amide and the “H from the nitrogen backbone

A

2

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18
Q

more than one polypeptide chain linked together

A

4

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19
Q

alpha helix

A

2

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20
Q

triple helix

A

4

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21
Q

slat bridges within a chain

A

3

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22
Q

hydrophobic interactions

A

3

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23
Q

disulfide bonding between chains

A

3

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24
Q

amino acid sequencing

A

1

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25
Q

beta sheets

A

2

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26
Q

albumin

A

Globular proteins

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27
Q

myosin

A

Fiberous proteins

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28
Q

collagen

A

Fiberous proteins

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29
Q

hemoglobin

A

Globular proteins

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30
Q

wool

A

Fiberous proteins

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31
Q

myoglobin

A

Globular proteins

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32
Q

silk

A

Fiberous proteins

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33
Q

serum globulins

A

Globular proteins

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34
Q

proteins used for structure

A

Fiberous proteins

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35
Q

proteins used for transportation

A

Globular proteins

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36
Q

proteins used for catalyzing reactions

A

Globular proteins

37
Q

proteins used of muscle contraction

A

Fiberous proteins

38
Q

Fiberous proteins

A

are used for structure

39
Q

Globular proteins

A

are fragile

used for enzymes and transportation

40
Q

which are most easily denatured

fiberous or globular proteins

A

globular proteins are easily denatured

41
Q

which has a greater solubility in aqueous solution, fibrous or globular protein

A

globular proteins are much more soluble than fiberous protiens

fiberous proteins are used for structural purposes

42
Q

how many poplypeptide chains are in:

myoglobin

A

1 chain

43
Q

how many poplypeptide chains are in:

hemoglobin

A

4 chains

44
Q

how many poplypeptide chains are in:

immunoglobulin

A

4 chains

45
Q

how many poplypeptide chains are in:

collagen

A

3 interwoven chains

46
Q

in a globular protein which amino acids would probably be found exclusively in the inside of the protein

A

Phenylalanine

Tryptophan

Glycine

47
Q

which protein is replaced the most often

A

enzymes

48
Q

which protein is replaced the least often

A

collagen

49
Q

threonine

serine

A

Hyrogen bonding

50
Q

valine

alanine

A

Hydrophobic interaction

51
Q

arginine

aspartic acid

A

salt linkages

52
Q

lysine

lysine

A

hydrogen bonding

53
Q

two cysteines

A

disulfide bonds

54
Q

arginine

glutamic acid

A

salt linkages

55
Q

phenylaline

isoleucine

A

hydrophobic interaction

56
Q

tyrosine

lysine

A

hydrogen bonding

57
Q

lysine

glutamic acid

A

salt bridge

58
Q

asparagine

lysine

A

hydrogen bonding

59
Q

glutamic acid

aspartic acid

A

hydrogen bonding

60
Q

arginine

tyrosine

A

hydrogen bonding

61
Q

aspartic acid

lysine

A

salt linkages

62
Q

phyenylalanine

alanine

A

hydrophobic interaction

63
Q

serine

lysine

A

hydrogen bonding

64
Q

tyrosine

glutamine

A

hydrogen bonding

65
Q

leucine

valine

A

hydrophobic interaction

66
Q

what amino acids have side chains that can help form salt bridges

A

glutamic acid or aspartic acid

with lysine or arginine

67
Q

transports oxygen in blood

A

hemoglobin

68
Q

destroys invading bacteria by breaking down its cell walls

A

lysozymes

69
Q

protein in silk

A

fibroin

70
Q

muscle protein used for movement

A

myosin

71
Q

stores oxygen in heart muscles

A

myoglobin

72
Q

hormone which regulates glucose metabolism

A

insulin

73
Q

antibody (combats infection)

A

immunoglobin

74
Q

protein in bone, connective tissue

A

collagen

75
Q

stores iron in the spleen

A

ferritin

76
Q

protein found in ligaments

A

elastin

77
Q

protein involved in blood clotting

A

thrombin

78
Q

protein that transports fatty acids

A

serum albumin

79
Q

polypeptide involved with water retention

A

vasopressin

80
Q

milk protein

A

casein

81
Q

protein in hair, nails, hooves

A

keratin

82
Q

blood protein which regulates osmotic pressure

A

serum albumin

83
Q

protein found in elastic tissue in artery wall

A

elastin

84
Q

poly peptide involved with lactation and induction of labor

A

oxytocin

85
Q

the fibrous protein which is very strong because of its triple helix structure

A

collagen

86
Q

the protein found in HDL or LDL

A

serum globulins

87
Q

most abundant protein in the human body

A

collagen

88
Q

proteins are least soluble at their isoelectric points. what would happen if a few drops of HCL were added to a protein which was already precipitated at is isoelectric point

A

the protein would begin to dissolve because the charges on the amino acid side chains would change. there would be more postivie charges than negative charges

Biochem (27 decks)

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