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

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

(124 cards)

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1
Q

Protein functions

A 
Catalyze (proteolysis)
Buffer
Storage (collagen)
Transport (Hgb)
Motion (Actin Myosin)
Structure (Collagen)
Defense (Antibodies) 
Regulation  (Hormones)
Transduce  (Receptors)
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2
Q

Protein functions

A 
Catalyze (proteolysis)
Buffer
Storage (collagen)
Transport (Hgb)
Motion (Actin Myosin)
Structure (Collagen)
Defense (Antibodies) 
Regulation  (Hormones)
Transduce  (Receptors)
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3
Q

Protein functions

A 
Catalyze (proteolysis)
Buffer
Storage (collagen)
Transport (Hgb)
Motion (Actin Myosin)
Structure (Collagen)
Defense (Antibodies) 
Regulation  (Hormones)
Transduce  (Receptors)
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4
Q

Protein functions

A 
Catalyze (proteolysis)
Buffer
Storage (collagen)
Transport (Hgb)
Motion (Actin Myosin)
Structure (Collagen)
Defense (Antibodies) 
Regulation  (Hormones)
Transduce  (Receptors)
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5
Q

Inhibits serine proteases

A

Alpha 1-Antitrypsin

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6
Q

Transmembrane protein Regulating Pigmentation in vertebrate organisms

A

Melanocortin 1 receptor

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7
Q

Nonpolar AA. “CALVIPPMTG”

A 
Cystein 
Alanine
Leucine
Valine
Isoleucine
Proline
Phenylalanine 
Methionine
Tryptophan
Glycine
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8
Q

Uncharged polar side chain AA

A

Asparagine

Glutamine

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9
Q

Basic Side Chains

A

Histidine Arginine Lysine

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10
Q

Acidic Side Chains

A

Aspartic Acid and Glutamic Acid

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11
Q

Polar AA

A 
Serine 
Threonine 
Asparagine 
Glutamine
Tyrosine
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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.

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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.

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14
Q

Essential AA

A

PVT TIM HLL

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15
Q

AA with OH groups hanging off of R group

A

Serine
Threonine
Tyrosine

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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

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17
Q

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

A

Glycine

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18
Q

Which type of reaction forms the disulfide bond?

A

Reduction

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19
Q

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

A

Highly charged

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20
Q

Site of N-glycosylation

A

Asparagine

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21
Q

More methyl groups mean more …

A

hydrophobic

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22
Q

Histone have lots of lysines .. why?

A

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

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23
Q

Collagen contains which two AA

A

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

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24
Q

Precursor of serotonin

A

Tryptophan

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25
Precursor of NO
Arginine
26
Precursor of Dopamine
Tyrosine
27
What does the formation of a peptide bond eliminate?
Water
28
Characteristics of the peptide bond
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
29
Overall charge at pH 7 Lys--Lys--Ser-Glu
Lys = +1 wins the H Lys = +1 wins the H Serine - unsure, but zero Glu = -1 overall = +1
30
Rotation of between N and Ca
phi
31
Rotation between Ca and CN
psi
32
The peptide bond retains polarity due to
migration of electrons from N to O
33
Protein is read
N--->C
34
Protein denaturing , you do what to it? Protein restoring function , you ?
Reduce it Oxidize it
35
Inhibits serine proteases
Alpha 1-Antitrypsin
36
Transmembrane protein Regulating Pigmentation in vertebrate organisms
Melanocortin 1 receptor
37
Nonpolar AA. "CALVIPPMTG"
``` Cystein Alanine Leucine Valine Isoleucine Proline Phenylalanine Methionine Tryptophan Glycine ```
38
Uncharged polar side chain AA
Asparagine | Glutamine
39
Basic Side Chains
Histidine Arginine Lysine
40
Acidic Side Chains
Aspartic Acid and Glutamic Acid
41
Polar AA
``` Serine Threonine Asparagine Glutamine Tyrosine ```
42
A side chain with a pH of 10.54 will not lose its proton in a physiological pH range. Why?
pKa is greater than pH, therefore pKa wins the hydrogens.
43
A side chain with pKa of 3.90 will lose its proton, but probably never get it back in physiological pH conditions. Why not?
pKa is lower than pH therefore the solution wins the protons.
44
Essential AA
PVT TIM HLL
45
AA with OH groups hanging off of R group
Serine Threonine Tyrosine
46
When cysteine has its proton it is (1.) and when it does not, it is (2.).
1. not very polar | 2. polar
47
Which AA can be hydrophobic, hydrophilic, and is also considered barely an AA?
Glycine
48
Which type of reaction forms the disulfide bond?
Reduction
49
When adding a phosphate to a molecule ,it makes it?
Highly charged
50
Site of N-glycosylation
Asparagine
51
More methyl groups mean more ...
hydrophobic
52
Histone have lots of lysines .. why?
Because they are hydrophobic and the histones need to be tightly packed.
53
Collagen contains which two AA
Glycine and proline . Proline contains OH to help make the fibrous structure.
54
Precursor of serotonin
Tryptophan
55
Precursor of NO
Arginine
56
Precursor of Dopamine
Tyrosine
57
What does the formation of a peptide bond eliminate?
Water
58
Characteristics of the peptide bond
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
Overall charge at pH 7 Lys--Lys--Ser-Glu
Lys = +1 wins the H Lys = +1 wins the H Serine - unsure, but zero Glu = -1 overall = +1
60
Rotation of between N and Ca
phi
61
Rotation between Ca and CN
psi
62
The peptide bond retains polarity due to
migration of electrons from N to O
63
Protein is read
N--->C
64
Protein denaturing , you do what to it? Protein restoring function , you ?
Reduce it Oxidize it
65
Inhibits serine proteases
Alpha 1-Antitrypsin
66
Transmembrane protein Regulating Pigmentation in vertebrate organisms
Melanocortin 1 receptor
67
Nonpolar AA. "CALVIPPMTG"
``` Cystein Alanine Leucine Valine Isoleucine Proline Phenylalanine Methionine Tryptophan Glycine ```
68
Uncharged polar side chain AA
Asparagine | Glutamine
69
Basic Side Chains
Histidine Arginine Lysine
70
Acidic Side Chains
Aspartic Acid and Glutamic Acid
71
Polar AA
``` Serine Threonine Asparagine Glutamine Tyrosine ```
72
A side chain with a pH of 10.54 will not lose its proton in a physiological pH range. Why?
pKa is greater than pH, therefore pKa wins the hydrogens.
73
A side chain with pKa of 3.90 will lose its proton, but probably never get it back in physiological pH conditions. Why not?
pKa is lower than pH therefore the solution wins the protons.
74
Essential AA
PVT TIM HLL
75
AA with OH groups hanging off of R group
Serine Threonine Tyrosine
76
When cysteine has its proton it is (1.) and when it does not, it is (2.).
1. not very polar | 2. polar
77
Which AA can be hydrophobic, hydrophilic, and is also considered barely an AA?
Glycine
78
Which type of reaction forms the disulfide bond?
Reduction
79
When adding a phosphate to a molecule ,it makes it?
Highly charged
80
Site of N-glycosylation
Asparagine
81
More methyl groups mean more ...
hydrophobic
82
Histone have lots of lysines .. why?
Because they are hydrophobic and the histones need to be tightly packed.
83
Collagen contains which two AA
Glycine and proline . Proline contains OH to help make the fibrous structure.
84
Precursor of serotonin
Tryptophan
85
Precursor of NO
Arginine
86
Precursor of Dopamine
Tyrosine
87
What does the formation of a peptide bond eliminate?
Water
88
Characteristics of the peptide bond
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
Overall charge at pH 7 Lys--Lys--Ser-Glu
Lys = +1 wins the H Lys = +1 wins the H Serine - unsure, but zero Glu = -1 overall = +1
90
Rotation of between N and Ca
phi
91
Rotation between Ca and CN
psi
92
The peptide bond retains polarity due to
migration of electrons from N to O
93
Protein is read
N--->C
94
Protein denaturing , you do what to it? Protein restoring function , you ?
Reduce it Oxidize it
95
Inhibits serine proteases
Alpha 1-Antitrypsin
96
Transmembrane protein Regulating Pigmentation in vertebrate organisms
Melanocortin 1 receptor
97
Nonpolar AA. "CALVIPPMTG"
``` Cystein Alanine Leucine Valine Isoleucine Proline Phenylalanine Methionine Tryptophan Glycine ```
98
Uncharged polar side chain AA
Asparagine | Glutamine
99
Basic Side Chains
Histidine Arginine Lysine
100
Acidic Side Chains
Aspartic Acid and Glutamic Acid
101
Polar AA
``` Serine Threonine Asparagine Glutamine Tyrosine ```
102
A side chain with a pH of 10.54 will not lose its proton in a physiological pH range. Why?
pKa is greater than pH, therefore pKa wins the hydrogens.
103
A side chain with pKa of 3.90 will lose its proton, but probably never get it back in physiological pH conditions. Why not?
pKa is lower than pH therefore the solution wins the protons.
104
Essential AA
PVT TIM HLL
105
AA with OH groups hanging off of R group
Serine Threonine Tyrosine
106
When cysteine has its proton it is (1.) and when it does not, it is (2.).
1. not very polar | 2. polar
107
Which AA can be hydrophobic, hydrophilic, and is also considered barely an AA?
Glycine
108
Which type of reaction forms the disulfide bond?
Reduction
109
When adding a phosphate to a molecule ,it makes it?
Highly charged
110
Site of N-glycosylation
Asparagine
111
More methyl groups mean more ...
hydrophobic
112
Histone have lots of lysines .. why?
Because they are hydrophobic and the histones need to be tightly packed.
113
Collagen contains which two AA
Glycine and proline . Proline contains OH to help make the fibrous structure.
114
Precursor of serotonin
Tryptophan
115
Precursor of NO
Arginine
116
Precursor of Dopamine
Tyrosine
117
What does the formation of a peptide bond eliminate?
Water
118
Characteristics of the peptide bond
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
Overall charge at pH 7 Lys--Lys--Ser-Glu
Lys = +1 wins the H Lys = +1 wins the H Serine - unsure, but zero Glu = -1 overall = +1
120
Rotation of between N and Ca
phi
121
Rotation between Ca and CN
psi
122
The peptide bond retains polarity due to
migration of electrons from N to O
123
Protein is read
N--->C
124
Protein denaturing , you do what to it? Protein restoring function , you ?
Reduce it Oxidize it

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

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