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
Phenylalanine Found in NutraSweet and anything with protein.
D. Phenylketonuria (PKU)
26
Treatment: Avoid phenylalanine in diet (low protein)
D. Phenylketonuria (PKU)
27
Genetic mutation that occurred over time to protect population from malaria but is Very Painful.
Sickle cell Anemia
28
• Valine (nonpolar) replaces glutamate (polar) in hemoglobin o Causing it to fold incorrectly.
Sickle cell Anemia
29
Sickle cell Anemia
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.)
30
used to make glucose, if necessary (product= Pyruvate)
Glucogenic
31
turned into Krebs cycle intermediate ketone bodies to fatty acids, if in excess (product= acetyl CoA)
Ketogenic
32
Glucogenic
used to make glucose, if necessary (product= Pyruvate)
33
Ketogenic
turned into Krebs cycle intermediate ketone bodies to fatty acids, if in excess (product= acetyl CoA)
34
Uncommon Amino Acids (found in collagen)
Hydroxyproline | Hydroxylysine
35
Uncommon Amino Acids (part of myosin)
Methyllysine
36
Uncommon Amino Acids (part of elastin)
Desmosine
37
Hydroxyproline | Hydroxylysine
Uncommon Amino Acids (found in collagen)
38
Methyllysine
Uncommon Amino Acids (part of myosin)
39
Desmosome
Uncommon Amino Acids (part of elastin)
40
Found in proteins that stimulate clotting and bone synthesis.
Carboxyglutamate
41
o A glutamate A.A with extra carboxylic acid.
Carboxyglutamate
42
Special A.A derivative that uses selenium instead of sulfur
Selenocysteine
43
Essential AA (branch chains)
Valine Isoleucine Leucine
44
Essential AA (base )
Histidine | Lysine
45
Presucurser for Histidine
Histamine
46
Presucurser for Lysine
Collagen
47
Presucurser for Leucine
Cholesterol
48
Presucurser for Methionine
SAMe
49
Essential AA (all of them)
``` Phenylalanine Valine Methionine Threonine Histidine Histamine Isoleucine Lysine  Leucine ```
50
derivates of Methionine
SAMe, sulfur containing precursor for S-adenosyl methionine ( needed for myelination)
51
derivates Proline
Collagen, Disrupts -α- helix and β-helix pleated sheet (secondary Structure) (Collagen loves it)
52
derivates Tyrosine
Thyroid hormones, melanin and catecholamines (dopamine, epinephrine and norepinephrine); Cell signaling.
53
derivates Serine
H-bonding
54
H-bonding
Serine
55
derivates Glutamic acids
GABA
56
GABA
Glutamic acids
57
derivates • Glutamine
Main N carrier
58
Derivates • Cysteine
Disulfide
59
Derivates • Tryptophan
melatonin, serotonin and niacin.
60
melatonin, serotonin and niacin.
Tryptophan
61
Main N carrier
Glutamine
62
Disulfide
Cysteine
63
Amphoteric
All have at least 2 charges at physiologic pH 
64
pH ↓ [H] ↑= AA can act as Bases
Proton acceptor
65
pH ↑ [H] ↓= AA can act as Acids
Proton Donor
66
Proton acceptor
pH ↓ [H] ↑= AA can act as Bases
67
Proton Donor
pH ↑ [H] ↓= AA can act as Acids
68
pH below pK
H is still attached-Pronated
69
pH above pK
H is lost deprotonated
70
Pronated
H is still attached | pH below pK
71
deprotonated
H is lost | pH above pK
72
pK1:
: removal of H from carboxyl group
73
pK2:
: removal of H from amino group
74
pKR:
Removal of H from R group
75
: removal of H from carboxyl group
pK1:
76
: removal of H from amino group
pK2:
77
Removal of H from R group
pKR:
78
What is a zwitterion is it good buffer at this point ?
The point where an amino acids or protein is neutral It not a good buffer at this point.
79
The point where an amino acids or protein is neutral
zwitterion
80
What does protonated
Pronated: H is attached
81
What does deprotonated mean?
Depronated: H is not attached.
82
How are peptide bonds formed?
• Dehydration run between N- terminal and of one AA and the C terminal of another AA
83
Chains of amino Acids
Peptides
84
Chains of amino Acids molecular weight>10,000
Proteins
85
Contains peptide bond formed by dehydration
Peptides
86
Contains peptide bonds
Proteins
87
Many amino acids is called polypeptide.
Peptides
88
Name the prosthetic group of lipoprotein, and give me an example?
Lipids | Example :VLDL
89
Name the prosthetic group of Glycoprotein,and give me an example?
Carbohydrates | example: Immunoglobulin G
90
Name the prosthetic group Phosphoproteins, and give me an example?
Phosphates example : Casein in milk
91
Name the prosthetic group Hemeproteins , and give me an example ?
Heme (protoporphyrin) | example: Hemoglobin
92
Name the prosthetic group Metalloproteins, and give me an example ?
Iron, zinc, calcium | Example : Ferritin, alcohol dehydration calmodulin.