Brainscape's Knowledge GenomeTM

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


See full index

Topnotch Biochemistry (Sept 2017) > Proteins > Flashcards

Proteins Flashcards

1
Q

Structure of Amino acid has 3 groups

A

Carboxyl Group Amino Group R Group

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

This structure dictates the function of the amino acid.

A

R group

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

Each amino acid has 3 common side group, except for ______

A

Proline : An Imino acid which lack the usual structure

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

Forms hydrophobic interactions: (A. Non-Polar | B. Polar Uncharged | C. Polar Charged )

A

A. Non-Polar

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

Found in the surface of proteins (A. Non-Polar | B. Polar Uncharged | C. Polar Charged )

A

Polar Uncharged and Charged

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

Forms ionic interaction: (A. Non-Polar | B. Polar Uncharged | C. Polar Charged )

A

C. Polar Charged

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

Forms hydrogen bonds: (A. Non-Polar | B. Polar Uncharged | C. Polar Charged )

A

B. Polar Uncharged

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
8
Q

Give 9 Non-Polar Amino acid

A

Glycine Alanine Valine Isoleucine Leucine Phenylalanine Tryptophan Methionine Proline

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

Give 3 Polar Uncharged -OH Amino acid

A

Serine Threonine Tyrosine

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

Polar uncharged -SH amino acid

A

Cysteine

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

Give 2 Negatively charged Amino acid at body pH

A

Aspartate Glutamate

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
12
Q

Give 2 Positively charged Amino acid at body pH

A

Arginine Lysine

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

Amino acid used in the first step of heme synthesis

A

Glycine

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

2 major free amino acids in the blood

A

Glycine and Alanine

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

3 amino acids whose metabolites accumulate in maple syrup urine disease

A

Valine Isoleucine Leucine

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

Carrier of ammonia and of carbons of pyruvate from skeletal muscle to liver

A

Alanine

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

Precursor of tyrosine

A

Phenylalanine

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

Interrupts a-helices in globular protein

A

Proline

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

Niacin: (Tryptophan or Tyrosine)

A

Tryptophan

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

Melanin (Tryptophan or Tyrosine)

A

Tyrosine

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

Thyroxine (Tryptophan or Tyrosine)

A

Tyrosine

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

Serotonin (Tryptophan or Tyrosine)

A

Tryptophan

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

Melatonin (Tryptophan or Tyrosine)

A

Tryptophan

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

Catecholamines (Tryptophan or Tyrosine)

A

Tyrosine

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

Smallest and Largest Amino Acid

A

Glycine and Tryptophan

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

Precursor of Urea

A

Arginine

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

Precursor of Histamine

A

Histidine

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

Amino acid used in FIGlu excretion test

A

Histidine

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

is the site for N-linked glycosylation of proteins

A

Asparagine

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

Participates in the biosynthesis of coenzyme A

A

Cysteine

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

Major carrier of nitrogen to liver from peripheral tissue

A

Glutamine

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

Component of keratin which contains a sulfhydryl group

A

Cysteine

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

Precursor for GABA and glutathione

A

Glutamate

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

A weak base and no charge amino acid at body pH

A

Histidine

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

21st amino acid

A

Selenocysteine

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

Present in Lathyrus seeds

A

Homoarginine and B-ODAP

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

Implicated in AML and found in cycad seeds

A

B-Methylaminoalanine

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
38
Q

All amino acids are chiral, except:

A

Glycine

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

More important configuration in amino acids

A

L-configuration

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

Define Zwitterion

A

Amino acids that bear no net charge at isoelectic pH

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

A semiessential amino acid

A

Arginine

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
42
Q

10 essential amino acids

A

Phenylalanine Valine Threonine Tryptophan Isoleucine Methionine Histidine Arginine Leucine Lysine (PVT TIM HAL always ARGues never TYRes)

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

Stepwise process of identifying the specific amino acid at each position in the peptide chain

A

Sequencing

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

1st protein whose sequence was determined by Sanger’s Reagent

A

Insulin Frederick Sanger, 1953

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

Reagent responsible for detachment of 1st AA in a sequence

A

Edman’s Reagent / Phenylisothiocynate

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

Reagent responsible for detachment of 2nd AA in a sequence

A

Sanger’s Reagent / 1-fluoro-2,4 dinitrobenzene

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

Determine protein’s aa sequence

A

Primary Structure

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

Primary structure is stabilized by _____ bonds.

A

Peptide bonds

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

Most common secondary structure

A

Apha Helix

50
Q

How many aa per turn of alpha helix

A

3.6 amino acids

51
Q

Where R groups of adjacent residues project in opposite directions

A

Beta Sheet

52
Q

Spiral structure with polypeptide backbone core with side chains extending outward

A

Alpha Helix

53
Q

Keratin (Alpha Helix or Beta Sheet or Motiffs)

A

Alpha Helix

54
Q

Hemoglobin (Alpha Helix or Beta Sheet or Motiffs)

A

Alpha Helix

55
Q

Amyloid (Alpha Helix or Beta Sheet or Motiffs)

A

Beta Sheet

56
Q

IgA (Alpha Helix or Beta Sheet or Motiffs)

A

Beta Sheet

57
Q

IgM (Alpha Helix or Beta Sheet or Motiffs)

A

Beta Sheet

58
Q

Greek Key (Alpha Helix or Beta Sheet or Motiffs)

A

Motiffs

59
Q

Supersecondary structures produced by packing side chains from adjacent secondary structural elements

A

Motiffs

60
Q

3 dimensional shape of a protein

A

Tertiary Structure

61
Q

Stabilized by hydrogen bonds

A

Secondary Structure

62
Q

Tertiary structure is stabilized by these 4 interactions

A

Disulfide bonds Hydrophobic interactions Hydrogen bonds Ionic interactions

63
Q

Functional and three dimensional structural units of polypeptide

A

Domains

64
Q

Specialized group of proteins required for the proper folding of many species of proteins

A

Chaperones

65
Q

Results in the unfolding and disorganization of the protein’s secondary and tertiary structures

A

Denaturation

66
Q

“Rescue” proteins

A

Chaperones

67
Q

Characteristics of Prion Disease

A

Spongiform changes Astrocytic gliomas Neuronal loss

68
Q

Apolipoprotein found in the chylomicron and Intermediate-density lipoprotein (IDLs) responsible for conformational transformation in Alzheimer Disease

A

ApoE

69
Q

Heme protein present in heart muscle

A

Myoglobin

70
Q

Shows hyperbolic O2 dissociation curve (Myoglobin or Hemoglobin)

A

Myoglobin

71
Q

Shows saturation (Myoglobin or Hemoglobin)

A

Myoglobin

72
Q

Present allosteric effects (Myoglobin or Hemoglobin)

A

Hemoglobin

73
Q

Shows sigmoidal O2 dissociation curve (Myoglobin or Hemoglobin)

A

Hemoglobin

74
Q

Single polypeptide (Myoglobin or Hemoglobin)

A

Myoglobin

75
Q

Factors that causes a shift to the RIGHT in O2 dissociation curve

A

INCREASE in: CO2 Acidity ( Dec pH) 2,3 BPG ( Inc altitude, HbF) Exercise Temperature

76
Q

Stabilizes the T structure of hgb

A

2, 3 BPG

77
Q

Explain Bohr Effect

A

Release of O2 from hgb is enganced when the pH is lowered or when hgb is in the presence of an increased pCO2

78
Q

Explain Haldane Effect

A

When less O2 is bound, the affinity of hemoglobin for CO2 increases

79
Q

Chains of Hb Gower 1

A

2 Sigma and 2 Epsilon chains

80
Q

Hb Gower 1 is produced in

A

Yolk Sac

81
Q

Chains of HbF

A

2 Alpha, 2 Gamma

82
Q

HbF is produced in

A

Liver

83
Q

Chains of HbA2

A

2 Alpha, 2 Delta

84
Q

Chains of HbA

A

2 Alpha, 2 Beta

85
Q

True or False. HbF has more affinity to O2 than HbA

A

True

86
Q

A1C goal for non pregnant adults

A

<7%.

87
Q

Treatment for Carboxyhemoglobinemia

A

100% O2 therapy

88
Q

“Chocolate cyanosis”

A

Methemoglobinemia

89
Q

Treatment for Acute mild Methemoglobinemia

A

Oral Methylene blue Ascorbic acid

90
Q

Most common mutation found in hereditary spherocytosis

A

Mutations in Ankyrin

91
Q

Hereditary spherocytosis is diagnosed using

A

Osmotic fragility test

92
Q

Treatment for hereditary spherocytosis

A

Splenectomy

93
Q

Results from a point mutation in both genes coding for the B-chain that results in a Valine rather than a glutamate amino acid

A

Sickle cell disease

94
Q

Clinical manifestation of Sickle cell disease

A

Painful crises Anemia Tissue anoxia

95
Q

In Hgb C disease what AA substitute glutamate

A

Lysine

96
Q

Inadequate synthesis of a-chains

A

Alpha Thalassemia

97
Q

Accumulation of HbBarts and a-chain precipitation

A

Beta Thalassemia

98
Q

Most abundant protein in the body

A

Collagen

99
Q

Collagen is stabilized by _______ bonds

A

Hydrogen

100
Q

Dentin (Collagen I, II, III, IV, VII)

A

Collagen I

101
Q

Nucleus pulposus (Collagen I, II, III, IV, VII)

A

Collagen II

102
Q

Late wound repair (Collagen I, II, III, IV, VII)

A

Collagen I

103
Q

Early wound repair (Collagen I, II, III, IV, VII)

A

Collagen III

104
Q

Basal Lamina (Collagen I, II, III, IV, VII)

A

Collagen IV

105
Q

Uterus (Collagen I, II, III, IV, VII)

A

Collagen III

106
Q

Fascia (Collagen I, II, III, IV, VII)

A

Collagen I

107
Q

Hematuria, Ocular lesions, Hearing loss > ERSD (Collagen I, II, III, IV, VII)

A

Collagen IV (Alport Syndrome)

108
Q

Dental imperfection, Hearing loss, Translucent connective tissue over choroidal veins. (Collagen I, II, III, IV, VII)

A

Collagen I (Osteogenesis Imperfecta)

109
Q

Most severe form of EDS (Collagen I, II, III, IV, VII)

A

Type III Fragile blood vessels and organs | Risk for aneurysms

110
Q

Impaired copper absorption and transport due to defective (ATP7A

A

Menkes disease

111
Q

Epidermolysis Bullosa (Collagen I, II, III, IV, VII)

A

Collagen VII

112
Q

Rich in proline and lysine with rubber like properties responsible for extensibility

A

Elastin

113
Q

Precursor tropoelastin is cross linked by _______

A

Desmosine

114
Q

Mutation found in dolichostenomelia + arachnodactyly + large vessel dilatation

A

Fibrillin 1 gene mutation. (Marfan syndrome)

115
Q

Type of emphysema found in A-1 antitrypsin deficienct

A

Panacinar

116
Q

Simplest protein

A

Protamine

117
Q

Type of interaction between non polar R groups

A

Hydrophobic interaction

118
Q

Type of interaction between charged amino acid

A

Ionic interaction

119
Q

All AA are optically active except

A

Glycine

120
Q

Inactive, larger form of proteases are called

A

Zymogens

121
Q

Most active amino group acceptor

A

Alpha-Ketoglutarate

122
Q

All amino acid can undergo transamination except: (2)

A

Lysine Threonine

Topnotch Biochemistry (Sept 2017) (9 decks)

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