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
beta sheets
2
26
albumin
Globular proteins
27
myosin
Fiberous proteins
28
collagen
Fiberous proteins
29
hemoglobin
Globular proteins
30
wool
Fiberous proteins
31
myoglobin
Globular proteins
32
silk
Fiberous proteins
33
serum globulins
Globular proteins
34
proteins used for structure
Fiberous proteins
35
proteins used for transportation
Globular proteins
36
proteins used for catalyzing reactions
Globular proteins
37
proteins used of muscle contraction
Fiberous proteins
38
Fiberous proteins
are used for structure
39
Globular proteins
are fragile | used for enzymes and transportation
40
which are most easily denatured fiberous or globular proteins
globular proteins are easily denatured
41
which has a greater solubility in aqueous solution, fibrous or globular protein
globular proteins are much more soluble than fiberous protiens fiberous proteins are used for structural purposes
42
how many poplypeptide chains are in: | myoglobin
1 chain
43
how many poplypeptide chains are in: | hemoglobin
4 chains
44
how many poplypeptide chains are in: | immunoglobulin
4 chains
45
how many poplypeptide chains are in: | collagen
3 interwoven chains
46
in a globular protein which amino acids would probably be found exclusively in the inside of the protein
Phenylalanine Tryptophan Glycine
47
which protein is replaced the most often
enzymes
48
which protein is replaced the least often
collagen
49
threonine serine
Hyrogen bonding
50
valine alanine
Hydrophobic interaction
51
arginine aspartic acid
salt linkages
52
lysine | lysine
hydrogen bonding
53
two cysteines
disulfide bonds
54
arginine glutamic acid
salt linkages
55
phenylaline isoleucine
hydrophobic interaction
56
tyrosine lysine
hydrogen bonding
57
lysine glutamic acid
salt bridge
58
asparagine lysine
hydrogen bonding
59
glutamic acid aspartic acid
hydrogen bonding
60
arginine tyrosine
hydrogen bonding
61
aspartic acid lysine
salt linkages
62
phyenylalanine alanine
hydrophobic interaction
63
serine lysine
hydrogen bonding
64
tyrosine glutamine
hydrogen bonding
65
leucine valine
hydrophobic interaction
66
what amino acids have side chains that can help form salt bridges
glutamic acid or aspartic acid | with lysine or arginine
67
transports oxygen in blood
hemoglobin
68
destroys invading bacteria by breaking down its cell walls
lysozymes
69
protein in silk
fibroin
70
muscle protein used for movement
myosin
71
stores oxygen in heart muscles
myoglobin
72
hormone which regulates glucose metabolism
insulin
73
antibody (combats infection)
immunoglobin
74
protein in bone, connective tissue
collagen
75
stores iron in the spleen
ferritin
76
protein found in ligaments
elastin
77
protein involved in blood clotting
thrombin
78
protein that transports fatty acids
serum albumin
79
polypeptide involved with water retention
vasopressin
80
milk protein
casein
81
protein in hair, nails, hooves
keratin
82
blood protein which regulates osmotic pressure
serum albumin
83
protein found in elastic tissue in artery wall
elastin
84
poly peptide involved with lactation and induction of labor
oxytocin
85
the fibrous protein which is very strong because of its triple helix structure
collagen
86
the protein found in HDL or LDL
serum globulins
87
most abundant protein in the human body
collagen
88
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
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