Proteins Flashcards
1
Q
Structure of Amino acid has 3 groups
A
Carboxyl Group Amino Group R Group
2
Q
This structure dictates the function of the amino acid.
A
R group
3
Q
Each amino acid has 3 common side group, except for ______
A
Proline : An Imino acid which lack the usual structure
4
Q
Forms hydrophobic interactions: (A. Non-Polar | B. Polar Uncharged | C. Polar Charged )
A
A. Non-Polar
5
Q
Found in the surface of proteins (A. Non-Polar | B. Polar Uncharged | C. Polar Charged )
A
Polar Uncharged and Charged
6
Q
Forms ionic interaction: (A. Non-Polar | B. Polar Uncharged | C. Polar Charged )
A
C. Polar Charged
7
Q
Forms hydrogen bonds: (A. Non-Polar | B. Polar Uncharged | C. Polar Charged )
A
B. Polar Uncharged
8
Q
Give 9 Non-Polar Amino acid
A
Glycine Alanine Valine Isoleucine Leucine Phenylalanine Tryptophan Methionine Proline
9
Q
Give 3 Polar Uncharged -OH Amino acid
A
Serine Threonine Tyrosine
10
Q
Polar uncharged -SH amino acid
A
Cysteine
11
Q
Give 2 Negatively charged Amino acid at body pH
A
Aspartate Glutamate
12
Q
Give 2 Positively charged Amino acid at body pH
A
Arginine Lysine
13
Q
Amino acid used in the first step of heme synthesis
A
Glycine
14
Q
2 major free amino acids in the blood
A
Glycine and Alanine
15
Q
3 amino acids whose metabolites accumulate in maple syrup urine disease
A
Valine Isoleucine Leucine
16
Q
Carrier of ammonia and of carbons of pyruvate from skeletal muscle to liver
A
Alanine
17
Q
Precursor of tyrosine
A
Phenylalanine
18
Q
Interrupts a-helices in globular protein
A
Proline
19
Q
Niacin: (Tryptophan or Tyrosine)
A
Tryptophan
20
Q
Melanin (Tryptophan or Tyrosine)
A
Tyrosine
21
Q
Thyroxine (Tryptophan or Tyrosine)
A
Tyrosine
22
Q
Serotonin (Tryptophan or Tyrosine)
A
Tryptophan
23
Q
Melatonin (Tryptophan or Tyrosine)
A
Tryptophan
24
Q
Catecholamines (Tryptophan or Tyrosine)
A
Tyrosine
25
Smallest and Largest Amino Acid
Glycine and Tryptophan
26
Precursor of Urea
Arginine
27
Precursor of Histamine
Histidine
28
Amino acid used in FIGlu excretion test
Histidine
29
is the site for N-linked glycosylation of proteins
Asparagine
30
Participates in the biosynthesis of coenzyme A
Cysteine
31
Major carrier of nitrogen to liver from peripheral tissue
Glutamine
32
Component of keratin which contains a sulfhydryl group
Cysteine
33
Precursor for GABA and glutathione
Glutamate
34
A weak base and no charge amino acid at body pH
Histidine
35
21st amino acid
Selenocysteine
36
Present in Lathyrus seeds
Homoarginine and B-ODAP
37
Implicated in AML and found in cycad seeds
B-Methylaminoalanine
38
All amino acids are chiral, except:
Glycine
39
More important configuration in amino acids
L-configuration
40
Define Zwitterion
Amino acids that bear no net charge at isoelectic pH
41
A semiessential amino acid
Arginine
42
10 essential amino acids
Phenylalanine Valine Threonine Tryptophan Isoleucine Methionine Histidine Arginine Leucine Lysine (PVT TIM HAL always ARGues never TYRes)
43
Stepwise process of identifying the specific amino acid at each position in the peptide chain
Sequencing
44
1st protein whose sequence was determined by Sanger's Reagent
Insulin Frederick Sanger, 1953
45
Reagent responsible for detachment of 1st AA in a sequence
Edman's Reagent / Phenylisothiocynate
46
Reagent responsible for detachment of 2nd AA in a sequence
Sanger's Reagent / 1-fluoro-2,4 dinitrobenzene
47
Determine protein's aa sequence
Primary Structure
48
Primary structure is stabilized by _____ bonds.
Peptide bonds
49
Most common secondary structure
Apha Helix
50
How many aa per turn of alpha helix
3.6 amino acids
51
Where R groups of adjacent residues project in opposite directions
Beta Sheet
52
Spiral structure with polypeptide backbone core with side chains extending outward
Alpha Helix
53
Keratin (Alpha Helix or Beta Sheet or Motiffs)
Alpha Helix
54
Hemoglobin (Alpha Helix or Beta Sheet or Motiffs)
Alpha Helix
55
Amyloid (Alpha Helix or Beta Sheet or Motiffs)
Beta Sheet
56
IgA (Alpha Helix or Beta Sheet or Motiffs)
Beta Sheet
57
IgM (Alpha Helix or Beta Sheet or Motiffs)
Beta Sheet
58
Greek Key (Alpha Helix or Beta Sheet or Motiffs)
Motiffs
59
Supersecondary structures produced by packing side chains from adjacent secondary structural elements
Motiffs
60
3 dimensional shape of a protein
Tertiary Structure
61
Stabilized by hydrogen bonds
Secondary Structure
62
Tertiary structure is stabilized by these 4 interactions
Disulfide bonds Hydrophobic interactions Hydrogen bonds Ionic interactions
63
Functional and three dimensional structural units of polypeptide
Domains
64
Specialized group of proteins required for the proper folding of many species of proteins
Chaperones
65
Results in the unfolding and disorganization of the protein's secondary and tertiary structures
Denaturation
66
"Rescue" proteins
Chaperones
67
Characteristics of Prion Disease
Spongiform changes Astrocytic gliomas Neuronal loss
68
Apolipoprotein found in the chylomicron and Intermediate-density lipoprotein (IDLs) responsible for conformational transformation in Alzheimer Disease
ApoE
69
Heme protein present in heart muscle
Myoglobin
70
Shows hyperbolic O2 dissociation curve (Myoglobin or Hemoglobin)
Myoglobin
71
Shows saturation (Myoglobin or Hemoglobin)
Myoglobin
72
Present allosteric effects (Myoglobin or Hemoglobin)
Hemoglobin
73
Shows sigmoidal O2 dissociation curve (Myoglobin or Hemoglobin)
Hemoglobin
74
Single polypeptide (Myoglobin or Hemoglobin)
Myoglobin
75
Factors that causes a shift to the RIGHT in O2 dissociation curve
INCREASE in: CO2 Acidity ( Dec pH) 2,3 BPG ( Inc altitude, HbF) Exercise Temperature
76
Stabilizes the T structure of hgb
2, 3 BPG
77
Explain Bohr Effect
Release of O2 from hgb is enganced when the pH is lowered or when hgb is in the presence of an increased pCO2
78
Explain Haldane Effect
When less O2 is bound, the affinity of hemoglobin for CO2 increases
79
Chains of Hb Gower 1
2 Sigma and 2 Epsilon chains
80
Hb Gower 1 is produced in
Yolk Sac
81
Chains of HbF
2 Alpha, 2 Gamma
82
HbF is produced in
Liver
83
Chains of HbA2
2 Alpha, 2 Delta
84
Chains of HbA
2 Alpha, 2 Beta
85
True or False. HbF has more affinity to O2 than HbA
True
86
A1C goal for non pregnant adults
\<7%.
87
Treatment for Carboxyhemoglobinemia
100% O2 therapy
88
"Chocolate cyanosis"
Methemoglobinemia
89
Treatment for Acute mild Methemoglobinemia
Oral Methylene blue Ascorbic acid
90
Most common mutation found in hereditary spherocytosis
Mutations in Ankyrin
91
Hereditary spherocytosis is diagnosed using
Osmotic fragility test
92
Treatment for hereditary spherocytosis
Splenectomy
93
Results from a point mutation in both genes coding for the B-chain that results in a Valine rather than a glutamate amino acid
Sickle cell disease
94
Clinical manifestation of Sickle cell disease
Painful crises Anemia Tissue anoxia
95
In Hgb C disease what AA substitute glutamate
Lysine
96
Inadequate synthesis of a-chains
Alpha Thalassemia
97
Accumulation of HbBarts and a-chain precipitation
Beta Thalassemia
98
Most abundant protein in the body
Collagen
99
Collagen is stabilized by _______ bonds
Hydrogen
100
Dentin (Collagen I, II, III, IV, VII)
Collagen I
101
Nucleus pulposus (Collagen I, II, III, IV, VII)
Collagen II
102
Late wound repair (Collagen I, II, III, IV, VII)
Collagen I
103
Early wound repair (Collagen I, II, III, IV, VII)
Collagen III
104
Basal Lamina (Collagen I, II, III, IV, VII)
Collagen IV
105
Uterus (Collagen I, II, III, IV, VII)
Collagen III
106
Fascia (Collagen I, II, III, IV, VII)
Collagen I
107
Hematuria, Ocular lesions, Hearing loss \> ERSD (Collagen I, II, III, IV, VII)
Collagen IV (Alport Syndrome)
108
Dental imperfection, Hearing loss, Translucent connective tissue over choroidal veins. (Collagen I, II, III, IV, VII)
Collagen I (Osteogenesis Imperfecta)
109
Most severe form of EDS (Collagen I, II, III, IV, VII)
Type III Fragile blood vessels and organs | Risk for aneurysms
110
Impaired copper absorption and transport due to defective (ATP7A
Menkes disease
111
Epidermolysis Bullosa (Collagen I, II, III, IV, VII)
Collagen VII
112
Rich in proline and lysine with rubber like properties responsible for extensibility
Elastin
113
Precursor tropoelastin is cross linked by \_\_\_\_\_\_\_
Desmosine
114
Mutation found in dolichostenomelia + arachnodactyly + large vessel dilatation
Fibrillin 1 gene mutation. (Marfan syndrome)
115
Type of emphysema found in A-1 antitrypsin deficienct
Panacinar
116
Simplest protein
Protamine
117
Type of interaction between non polar R groups
Hydrophobic interaction
118
Type of interaction between charged amino acid
Ionic interaction
119
All AA are optically active except
Glycine
120
Inactive, larger form of proteases are called
Zymogens
121
Most active amino group acceptor
Alpha-Ketoglutarate
122
All amino acid can undergo transamination except: (2)
Lysine Threonine
