Brainscape's Knowledge GenomeTM

Browse over 1 million classes created by top students, professors, publishers, and experts.


See full index

Block 1 -Test 1, (Biochem) > Lecture 3 (8/17) -Amino Acids and Proteins > Flashcards

Lecture 3 (8/17) -Amino Acids and Proteins Flashcards

1
Q

Protein functions

A 
Catalyze (proteolysis)
Buffer
Storage (collagen)
Transport (Hgb)
Motion (Actin Myosin)
Structure (Collagen)
Defense (Antibodies) 
Regulation  (Hormones)
Transduce  (Receptors)
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
2
Q

Protein functions

A 
Catalyze (proteolysis)
Buffer
Storage (collagen)
Transport (Hgb)
Motion (Actin Myosin)
Structure (Collagen)
Defense (Antibodies) 
Regulation  (Hormones)
Transduce  (Receptors)
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
3
Q

Protein functions

A 
Catalyze (proteolysis)
Buffer
Storage (collagen)
Transport (Hgb)
Motion (Actin Myosin)
Structure (Collagen)
Defense (Antibodies) 
Regulation  (Hormones)
Transduce  (Receptors)
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
4
Q

Protein functions

A 
Catalyze (proteolysis)
Buffer
Storage (collagen)
Transport (Hgb)
Motion (Actin Myosin)
Structure (Collagen)
Defense (Antibodies) 
Regulation  (Hormones)
Transduce  (Receptors)
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
5
Q

Inhibits serine proteases

A

Alpha 1-Antitrypsin

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
6
Q

Transmembrane protein Regulating Pigmentation in vertebrate organisms

A

Melanocortin 1 receptor

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
7
Q

Nonpolar AA. “CALVIPPMTG”

A 
Cystein 
Alanine
Leucine
Valine
Isoleucine
Proline
Phenylalanine 
Methionine
Tryptophan
Glycine
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
8
Q

Uncharged polar side chain AA

A

Asparagine

Glutamine

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
9
Q

Basic Side Chains

A

Histidine Arginine Lysine

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
10
Q

Acidic Side Chains

A

Aspartic Acid and Glutamic Acid

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
11
Q

Polar AA

A 
Serine 
Threonine 
Asparagine 
Glutamine
Tyrosine
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
12
Q

A side chain with a pH of 10.54 will not lose its proton in a physiological pH range. Why?

A

pKa is greater than pH, therefore pKa wins the hydrogens.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
13
Q

A side chain with pKa of 3.90 will lose its proton, but probably never get it back in physiological pH conditions. Why not?

A

pKa is lower than pH therefore the solution wins the protons.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
14
Q

Essential AA

A

PVT TIM HLL

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
15
Q

AA with OH groups hanging off of R group

A

Serine
Threonine
Tyrosine

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
16
Q

When cysteine has its proton it is (1.) and when it does not, it is (2.).

A
  1. not very polar

2. polar

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
17
Q

Which AA can be hydrophobic, hydrophilic, and is also considered barely an AA?

A

Glycine

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
18
Q

Which type of reaction forms the disulfide bond?

A

Reduction

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
19
Q

When adding a phosphate to a molecule ,it makes it?

A

Highly charged

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
20
Q

Site of N-glycosylation

A

Asparagine

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
21
Q

More methyl groups mean more …

A

hydrophobic

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
22
Q

Histone have lots of lysines .. why?

A

Because they are hydrophobic and the histones need to be tightly packed.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
23
Q

Collagen contains which two AA

A

Glycine and proline . Proline contains OH to help make the fibrous structure.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
24
Q

Precursor of serotonin

A

Tryptophan

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
25
Q

Precursor of NO

A

Arginine

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
26
Q

Precursor of Dopamine

A

Tyrosine

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
27
Q

What does the formation of a peptide bond eliminate?

A

Water

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
28
Q

Characteristics of the peptide bond

A

Planar -6 atoms are fixed in a plane

Partial double bond

Partial charge

Trans-all R groups are on the opposite side of each other .

Limits degree of freedom

Decrease in entropy

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
29
Q

Overall charge at pH 7

Lys–Lys–Ser-Glu

A

Lys = +1 wins the H
Lys = +1 wins the H
Serine - unsure, but zero
Glu = -1

overall = +1

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
30
Q

Rotation of between N and Ca

A

phi

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
31
Q

Rotation between Ca and CN

A

psi

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
32
Q

The peptide bond retains polarity due to

A

migration of electrons from N to O

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
33
Q

Protein is read

A

N—>C

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
34
Q

Protein denaturing , you do what to it?

Protein restoring function , you ?

A

Reduce it

Oxidize it

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
35
Q

Inhibits serine proteases

A

Alpha 1-Antitrypsin

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
36
Q

Transmembrane protein Regulating Pigmentation in vertebrate organisms

A

Melanocortin 1 receptor

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
37
Q

Nonpolar AA. “CALVIPPMTG”

A 
Cystein 
Alanine
Leucine
Valine
Isoleucine
Proline
Phenylalanine 
Methionine
Tryptophan
Glycine
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
38
Q

Uncharged polar side chain AA

A

Asparagine

Glutamine

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
39
Q

Basic Side Chains

A

Histidine Arginine Lysine

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
40
Q

Acidic Side Chains

A

Aspartic Acid and Glutamic Acid

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
41
Q

Polar AA

A 
Serine 
Threonine 
Asparagine 
Glutamine
Tyrosine
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
42
Q

A side chain with a pH of 10.54 will not lose its proton in a physiological pH range. Why?

A

pKa is greater than pH, therefore pKa wins the hydrogens.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
43
Q

A side chain with pKa of 3.90 will lose its proton, but probably never get it back in physiological pH conditions. Why not?

A

pKa is lower than pH therefore the solution wins the protons.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
44
Q

Essential AA

A

PVT TIM HLL

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
45
Q

AA with OH groups hanging off of R group

A

Serine
Threonine
Tyrosine

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
46
Q

When cysteine has its proton it is (1.) and when it does not, it is (2.).

A
  1. not very polar

2. polar

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
47
Q

Which AA can be hydrophobic, hydrophilic, and is also considered barely an AA?

A

Glycine

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
48
Q

Which type of reaction forms the disulfide bond?

A

Reduction

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
49
Q

When adding a phosphate to a molecule ,it makes it?

A

Highly charged

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
50
Q

Site of N-glycosylation

A

Asparagine

51
Q

More methyl groups mean more …

A

hydrophobic

52
Q

Histone have lots of lysines .. why?

A

Because they are hydrophobic and the histones need to be tightly packed.

53
Q

Collagen contains which two AA

A

Glycine and proline . Proline contains OH to help make the fibrous structure.

54
Q

Precursor of serotonin

A

Tryptophan

55
Q

Precursor of NO

A

Arginine

56
Q

Precursor of Dopamine

A

Tyrosine

57
Q

What does the formation of a peptide bond eliminate?

A

Water

58
Q

Characteristics of the peptide bond

A

Planar -6 atoms are fixed in a plane

Partial double bond

Partial charge

Trans-all R groups are on the opposite side of each other .

Limits degree of freedom

Decrease in entropy

59
Q

Overall charge at pH 7

Lys–Lys–Ser-Glu

A

Lys = +1 wins the H
Lys = +1 wins the H
Serine - unsure, but zero
Glu = -1

overall = +1

60
Q

Rotation of between N and Ca

A

phi

61
Q

Rotation between Ca and CN

A

psi

62
Q

The peptide bond retains polarity due to

A

migration of electrons from N to O

63
Q

Protein is read

A

N—>C

64
Q

Protein denaturing , you do what to it?

Protein restoring function , you ?

A

Reduce it

Oxidize it

65
Q

Inhibits serine proteases

A

Alpha 1-Antitrypsin

66
Q

Transmembrane protein Regulating Pigmentation in vertebrate organisms

A

Melanocortin 1 receptor

67
Q

Nonpolar AA. “CALVIPPMTG”

A 
Cystein 
Alanine
Leucine
Valine
Isoleucine
Proline
Phenylalanine 
Methionine
Tryptophan
Glycine
68
Q

Uncharged polar side chain AA

A

Asparagine

Glutamine

69
Q

Basic Side Chains

A

Histidine Arginine Lysine

70
Q

Acidic Side Chains

A

Aspartic Acid and Glutamic Acid

71
Q

Polar AA

A 
Serine 
Threonine 
Asparagine 
Glutamine
Tyrosine
72
Q

A side chain with a pH of 10.54 will not lose its proton in a physiological pH range. Why?

A

pKa is greater than pH, therefore pKa wins the hydrogens.

73
Q

A side chain with pKa of 3.90 will lose its proton, but probably never get it back in physiological pH conditions. Why not?

A

pKa is lower than pH therefore the solution wins the protons.

74
Q

Essential AA

A

PVT TIM HLL

75
Q

AA with OH groups hanging off of R group

A

Serine
Threonine
Tyrosine

76
Q

When cysteine has its proton it is (1.) and when it does not, it is (2.).

A
  1. not very polar

2. polar

77
Q

Which AA can be hydrophobic, hydrophilic, and is also considered barely an AA?

A

Glycine

78
Q

Which type of reaction forms the disulfide bond?

A

Reduction

79
Q

When adding a phosphate to a molecule ,it makes it?

A

Highly charged

80
Q

Site of N-glycosylation

A

Asparagine

81
Q

More methyl groups mean more …

A

hydrophobic

82
Q

Histone have lots of lysines .. why?

A

Because they are hydrophobic and the histones need to be tightly packed.

83
Q

Collagen contains which two AA

A

Glycine and proline . Proline contains OH to help make the fibrous structure.

84
Q

Precursor of serotonin

A

Tryptophan

85
Q

Precursor of NO

A

Arginine

86
Q

Precursor of Dopamine

A

Tyrosine

87
Q

What does the formation of a peptide bond eliminate?

A

Water

88
Q

Characteristics of the peptide bond

A

Planar -6 atoms are fixed in a plane

Partial double bond

Partial charge

Trans-all R groups are on the opposite side of each other .

Limits degree of freedom

Decrease in entropy

89
Q

Overall charge at pH 7

Lys–Lys–Ser-Glu

A

Lys = +1 wins the H
Lys = +1 wins the H
Serine - unsure, but zero
Glu = -1

overall = +1

90
Q

Rotation of between N and Ca

A

phi

91
Q

Rotation between Ca and CN

A

psi

92
Q

The peptide bond retains polarity due to

A

migration of electrons from N to O

93
Q

Protein is read

A

N—>C

94
Q

Protein denaturing , you do what to it?

Protein restoring function , you ?

A

Reduce it

Oxidize it

95
Q

Inhibits serine proteases

A

Alpha 1-Antitrypsin

96
Q

Transmembrane protein Regulating Pigmentation in vertebrate organisms

A

Melanocortin 1 receptor

97
Q

Nonpolar AA. “CALVIPPMTG”

A 
Cystein 
Alanine
Leucine
Valine
Isoleucine
Proline
Phenylalanine 
Methionine
Tryptophan
Glycine
98
Q

Uncharged polar side chain AA

A

Asparagine

Glutamine

99
Q

Basic Side Chains

A

Histidine Arginine Lysine

100
Q

Acidic Side Chains

A

Aspartic Acid and Glutamic Acid

101
Q

Polar AA

A 
Serine 
Threonine 
Asparagine 
Glutamine
Tyrosine
102
Q

A side chain with a pH of 10.54 will not lose its proton in a physiological pH range. Why?

A

pKa is greater than pH, therefore pKa wins the hydrogens.

103
Q

A side chain with pKa of 3.90 will lose its proton, but probably never get it back in physiological pH conditions. Why not?

A

pKa is lower than pH therefore the solution wins the protons.

104
Q

Essential AA

A

PVT TIM HLL

105
Q

AA with OH groups hanging off of R group

A

Serine
Threonine
Tyrosine

106
Q

When cysteine has its proton it is (1.) and when it does not, it is (2.).

A
  1. not very polar

2. polar

107
Q

Which AA can be hydrophobic, hydrophilic, and is also considered barely an AA?

A

Glycine

108
Q

Which type of reaction forms the disulfide bond?

A

Reduction

109
Q

When adding a phosphate to a molecule ,it makes it?

A

Highly charged

110
Q

Site of N-glycosylation

A

Asparagine

111
Q

More methyl groups mean more …

A

hydrophobic

112
Q

Histone have lots of lysines .. why?

A

Because they are hydrophobic and the histones need to be tightly packed.

113
Q

Collagen contains which two AA

A

Glycine and proline . Proline contains OH to help make the fibrous structure.

114
Q

Precursor of serotonin

A

Tryptophan

115
Q

Precursor of NO

A

Arginine

116
Q

Precursor of Dopamine

A

Tyrosine

117
Q

What does the formation of a peptide bond eliminate?

A

Water

118
Q

Characteristics of the peptide bond

A

Planar -6 atoms are fixed in a plane

Partial double bond

Partial charge

Trans-all R groups are on the opposite side of each other .

Limits degree of freedom

Decrease in entropy

119
Q

Overall charge at pH 7

Lys–Lys–Ser-Glu

A

Lys = +1 wins the H
Lys = +1 wins the H
Serine - unsure, but zero
Glu = -1

overall = +1

120
Q

Rotation of between N and Ca

A

phi

121
Q

Rotation between Ca and CN

A

psi

122
Q

The peptide bond retains polarity due to

A

migration of electrons from N to O

123
Q

Protein is read

A

N—>C

124
Q

Protein denaturing , you do what to it?

Protein restoring function , you ?

A

Reduce it

Oxidize it

Block 1 -Test 1, (Biochem) (12 decks)

Brainscape helps you reach your goals faster, through stronger study habits.
© 2024 Bold Learning Solutions. Terms and Conditions