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Biochemistry by mgcMD > Proteins > Flashcards

Proteins Flashcards

1
Q

Linear polymers of amino acids

A

Proteins

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2
Q

Set of all proteins expressed by an individual cell at a particular time

A

Proteome

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3
Q

3 groups that comprise the basic structure of amino acids except proline

A

Carboxyl group
Amino group
R group (distinctive side chain)

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4
Q

Non polar amino acids

A 
Glycine
Alanine
Valine
Isoleucine
Leucine
Phenylalanine
Tryptophan
Methionine
Proline
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5
Q

Polar uncharged AAs

A

-OH
Serine
Threonin
Tyrosine

-SH
Cysteine

Amide
Asparagi e
Glutamine

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6
Q

Charged AAs

A

Acidic
Aspartate
Glutamate

Basic
Arginine
Lysine
Histidine

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7
Q

Group of AA that have zero net charged
Forms hydrophobic interactions
Found in the interior of protein

A

Non-polar AA

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8
Q

Group of AAs that have zero net charge
Forms hydrogen bonds
Found in the surface if a protein

A

Polar uncharged AA

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9
Q

Group of AA that have positive or negative net charge (acidic or basic)
Forms ionic interactions
Found in the surface of a protein

A

Charged AA

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10
Q

Identify AA
has the smallest side chain
Used in the first step of heme synthesis
Used in synthesis if purines and creatine
Conjugated to bile acids, drugs, and other metabolites
Major inhibitory transmitter in the spinal cord

A

Glycine

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11
Q

Identify AA

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

A

Alanine

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12
Q

Identify AA

Together with glycine, contitutes a major fraction if free amino acids in the blood

A

Alanine

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13
Q

Branched chain amino acids whose metabolites accumulate in MSUD

A

Valine
Leucine
Isoleucine

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14
Q

Identify AA

Precursor of tyrosine that accumulated in PKU

A

Phenylalanine

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15
Q

AA with largest side chain

A

Tryptophan

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16
Q

AA precursor of niacin, serotonin, melatonin

A

Tryptophan

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17
Q

AA
Source of methyl groups in metabolism
Involve in the transfer if methyl groups as S-adenosylmethionine (SAM)

A

Methionine

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18
Q

AA

Precursor of homocysteine and cysteine

A

Methionine

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19
Q

AA

Not an amino acid, but an imino acid

A

Proline

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20
Q

AA

Contributes to the fibrous structure of collagen and interrupts alpha helices in globular proteins

A

Proline

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21
Q

Uncharged polar amino acids that contain hydroxyl group

A

Serine
Threonine
Tyrosine

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22
Q

AA

Site for O-linked glycosylation and phosphorylation of proteins

A

Serine
Threonine
Tyrosine

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23
Q

AA precursor of thyroxine and melanin

A

Tyrosine

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24
Q

Fill in

Phenylalanine—>______ —> L Dopa —> _____ —>norepinephrine —-> _____

A

Tyrosine
Dopamine
Epinephrine

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25
Q

AA

Site for N-linked glycosylation of proteins

A

Asparagine

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26
Q

AA
When deaminated, it results to formation of ammonia, and is a major carrier of nitrogen to the liver from peripheral tissues

A

Glutamine

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27
Q

AA

Contains sulfhydryl group that is an active part of many enzymes

A

Cysteine

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28
Q

AA
Participates in the biosynthesis of coenzyme A
Keratin contains a lot of its derivative

A

Cysteine

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29
Q

2 AA
Negatively charged at neutral pH due to the carboxylate group
Serve as proton donors
Participate in ionic interactions

A

Glutamate, Aspartate

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30
Q

AA

Precursor for GABA and glutathione

A

Glutamate

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31
Q

Name 3 basic AA

A

Histidine
Arginine
Lysine

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32
Q

At neutral pH,
Arginine and lysine are (+/-) charged
Histidine, being a weak base, has ___ charge

A

+

Zero

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33
Q

AA

Precursor of histamine

A

Histidine

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34
Q

AA
Used in the diagnosis of folic acid deficiency (FIGlu excretion test)
Concentration in the brain varies with circadian rhythm

A

Histidine

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35
Q

Histidine—> (histidinase) —> FIGLU

FIGlu —>______ —> glutamate

A

Tetrahydrofolate

Folate deficiency elevates urine FIGlu with oral histidine load

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36
Q

AA

precursor of creatine, urea, and NO

A

Arginine

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37
Q

AA

Precursor of carnitine

A

Lysine

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38
Q

21st amino acid

A

Selenocysteine

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39
Q

AA found in a handful of proteins, including certain peroxidases and reductases, where it participates in the catalysis of electron transfer reactions

A

Selenocysteine

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40
Q

A selenium ion replaces the ____ component of its structural analog, cysteine

A

Sulfur

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41
Q

AA that is inserted into polypeptide during translation but is not specified by a simple three-letter codon

A

Selenocysteine

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42
Q

Plant L alpha amino acid
Present in Lathyrus seeds
Implicated in neurolathyrism
Characterized by progressive and irreversible spastic paralysis of the lower extremities

A

Homoarginine and BETA ODAP

Oxalyldiaminopropionic acid

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43
Q

Neurotoxic amino acid in cycad seeds

A

Beta methylaminoalanine

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44
Q

AA in cycad seeds impkicated in neurodegenerative diseases, includinf amyotropic lateral sclerosis Parkinson dementia complex in natives if Guam

A

Beta methylaminoalanin

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45
Q

Except for ____ all AA are chiral

A

Glycine

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46
Q

All amino acids in proteins are in what configuration

A

L configuration

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47
Q

Amino acods in bacterial cell walls and antibiotiuvs are in what configuration

A

D configurarion

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48
Q

Term that denotes an amino acid that bears no net charge at its isoelectric pH (pI)

A

Zwitterion

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49
Q

Essential amino acids

A 
Phenylalanine
Valine
Tryptophan
Threonine
 Isoleucine
Methionine
Histidine
Arginine
Leucine
Lysine
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50
Q

AA that is considered nutritionally semiessential

A

Arginine

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51
Q

2 AA that can be synthesized in the body, but only from essential amino acid precursors

A

Cystine

Tyrosine

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52
Q

Stucture of protein determined by a protein’s amino acid sequence

A

Primary structure

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53
Q

_______ bonds attach the amino group of one amino to the alpha carbonyl group of another

A

Peptide

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54
Q

Peptide bonds have
Partial (double/single) bond character
(Rigid/non-rigid) and planar
Generally in the (cis/trans) configuration
Disrup by (what process) through prolonged exposure to a strong acid or base

A

Double bond
Rigid
Trans
Hydrolysis

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55
Q

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

A

Sequencing

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56
Q

2 reagents used for sequencing AA

From N-terminal AA

A

Sanger’s reagent (1-fluoro-2,4-dinitribenzene)

Edman’s reagent (phenylisothiocyanate)

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57
Q

2 Reagents used for AA sequencing

From c-terminal amino acid

A

Hydralazine

Carboxypeptidase

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58
Q

Level of protein stucture described as folding of short (3-30 residue) contiguous segments of polypeptide into geometrically ordered units

A

Secondary structure

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59
Q

Level of protein structure stabilized by Hydrogen bonding

A

Secondary

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60
Q

Secondary protein structure is stabilized by

A

Hydrogen bonds

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61
Q

2 forms of secondary stucture

A

Alpha helix

Beta sheet

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62
Q

More common form of secondary protein structure

A

Alpha helix

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63
Q

Form of secondary protein structure

Spiral, with polypeptide backbone core, with side chains extending outward

A

Alpha helix

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64
Q

How many AA per turn in alpha helix protein stucture

A

3.66

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65
Q

Alpha helix protein structure is disrupted by what

A

Proline, AAS with large or charged R groups

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66
Q

Keratin and hemoglobin are examples of proteins in what structure

A

Alpha helix (secondary structure)

Keratin (100% alpha helix)
Hemiglobin (80% alpha helix)

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67
Q

Protein structure wherein AA residues form a zigzagor pleated pattern

A

Beta sheet

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68
Q

In beta sheet protein stucture, R groups of adjacent residues project in (opposite/same) directions

A

Opposite

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69
Q

Amyloid and immunoglobulin are examples of proteins in what structure?

A

Beta sheet (secondary)

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70
Q

These are protein structures with less regukar configuration forming loops and bends

A

Non- repetitive secondary structures

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71
Q

______ are supersecondary structures produced by packing side chains from adjacent secondary structural elements close to each other

A

Motifs

Examples are beta-alpha-beta unit
Greek key
Beta meander
Beta barrel

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72
Q

Overall 3-dimensional shape of protein

Includes globular and fibrous proteins

A

Tertiary structure

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73
Q

The assembly of secondary structural units into larger functional units such as the mature polypeptide and its component domains

A

Tertiary structure

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74
Q

4 bonds/interactions that stabilize tertiary protein structure

A

Disulfide bonds
Hydrophobic interactions
Hydrogen bonds
Ionic interactions

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75
Q

Fundamental functional and three dimensional structural units of polypeptide

A

Domains

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76
Q

Level of protein structure

Number and types of polypeptide units oligomeric proteins and their spatial arrangements

A

Quaternary structure

77
Q

Protein stucture that includes
monomeric vs dimeric
Homidimers vs heterodimers

A

Quaternary stucture

78
Q

Specialized group of proteins required for the proper folding of many species of proteins
Prevents aggregation, paves the way for the formation of appropriate secondary structural elements and their subsequent coalescence into a molten globule

A

Chaperones

79
Q

Specialized group if proteins that can rescue other proteins that have become thermodynamically trapped in a misfolded dead end by unfolding hydrophobic regions

A

Chaperones

80
Q

Process that results in the unfolding and disorganization of the proteins secondary and tertiary structures

A

Denaturation

81
Q

Protein stuctures destroyed by denaturation

A

Secondary and tertiary

82
Q

T/F protein denaturation is accompanied by hydrolysis of peptide bonds

A

F

83
Q

T/F protein denaturation may be reversibel, but most proteins remain permanently disordered

A

T

84
Q

Fatal neurodegenrative diseases characterized by spongiform changes, astrocytic gliomas, and neuronal loss resulting from the deposition of insoluble protein aggregates in neural cells

A

Prion Diseases

85
Q

T/F prion diseases can be transmitted by protein alone, without involvement of DNA or RNA

A

T

86
Q

Re Prion Dses:
An altered version of a protein converts normal protein (PrPc, rich in ______) to the pathognomonic conformation (PrPsc, rich in _____)

A

Alpha helices

Beta sheets

87
Q

Disease characterized with senile plaques and neurofibrillary tangles that contain aggregates of protein beta amyloid

A

Alzheimers dse

88
Q

In Alzheimers dse, B amyloid becomes elevated, and this protein undergoes a conformational change from a soluble alpha helix rich state in beta sheets prone to self-aggregation

A

Alzheimer

89
Q

Conformational transformation of protein in alzheimers dse is implicated to_____^

A

Apolipoprotein E

90
Q

Examples of globular proteins

A

Hemoglobin

Myoglobin

91
Q

Hemoglobin form with low oxygen affinity

A

Taut form

92
Q

Hemiglobin form with high oxygen affinity

A

R (relaxed) form

93
Q

This principle states that hemoglobin binds up to 4 molecules of oxygen with increasing affinity

A

Positive cooperativity

94
Q

Heme protein found exclusively in RBC

A

Hemoglobin

95
Q

Heme protein present in heart and skeletal muscle

A

Myoglobin

96
Q

Reservoir of oxygen

Oxygen carrier that increase the rate of transport of oxygen within the muscle

A

Myoglobin

97
Q

Myoglobin/Hemoglobin

1 polypeptide

A

Myoglobin

98
Q

Myoglobin/Hemoglobin

4 polypeptides

A

Hemoglobin

99
Q

Myoglobin/Hemoglobin

Binds to 1 oxygen only

A

Myoglobin

100
Q

Myoglobin/Hemoglobin

Binds ro 4 oxygen molecules

A

Hemoglobin

101
Q

Myoglobin/Hemoglobin

Hyperbolic oxygen dissociation curve

A

Myoglobin

102
Q

Myoglobin/Hemoglobin
Oxygen dissociation curve id sigmoidal
Demonstrates cooperativity

A

Hemoglobin

103
Q

Myoglobin/Hemoglobin

Oxygen storage

A

Myoglobin

104
Q

Myoglobin/Hemoglobin

Oxygen transport

A

Hemoglobin

105
Q

Myoglobin/Hemoglobin

Absent allosteric effects

A

Myoglobin

106
Q

Myoglobin/Hemoglobin

Present allosteric effects

A

Hemoglobin

107
Q

Factors that shift O2-Hgb dissociation curve to the right

A 
CO2
Acidity
2,3 BPG
Exercise
Temperature
108
Q

Stabilizes the T structure of hemoglobin by fprming additional salt bridges that must be broken prior to conversion to the R state

A

2, 3 BPG

109
Q

T/F

In infants, 2,3 BPG binds more weakly to HbF than to HbA. Hence, HbF has higher affinity to oxygen than HbA

A

T

110
Q

T/F
Prolonged exposure to high altitude increases the number of erythrocytes. Hence, increased hemoglobin and increased BPG lowers the affinity of HbA for 02

A

T

111
Q

A low pO2 in peripheral tissues (promotes/inhibits) the synthesis in erythrocytes of 2,3 BPG from the glycolytic intermediate 1,3 BPG

A

Promotes

112
Q

This effect describes that the release of oxygen from hemoglobin is increased when the pH is lowered or when the hemoglobin is in the presence of increased pCO2

A

BOHR effect

113
Q

T/F

Oxyhemoglobin has greater affinity for protons than does deoxy form

A

F

114
Q

The effect of changes in hemoglobin saturation on the relationship of CO2 content to PCO2

A

Haldane effect

115
Q

Minor type of hemoglobin

Produced from conception to first few months

A

Embryonal hemoglobin

Hb Gower 1

116
Q

Hb Gower 1

(Embryonal Hemoglobin) is synthesized where?

A

Yolk Sac

117
Q

Identify minor hemoglobin

Alpha2gamma2

A

Fetal hemoglobin

HbF

118
Q

Minor Hgb synthesized first few months to after birth

A

HbF (Fetal Hgb)

119
Q

Minor Hgb synthesized in the liver

A

HbF (Fetal Hemoglobin)

120
Q

Minor hgb with alpha2 beta 2 chains

A

HbA

Hemoglobin A

121
Q

Minor hemoglobin synthesized 8 months and onwards

A

HbA

122
Q

Minor hemoglobin synthesized in marrow

A

HbA and HbA2

123
Q

Minor Hgb

Alpha2 delta 2

A

HbA2

124
Q

Minor Hgb synthesized shortly after birth onwards

A

HbA2

125
Q

Site if synthesis of HbA2

A

Marrow

126
Q

Major Hgb found in fetus

Has increased affinity doe oxygen than HbA

A

Fetal Hgb

HbF

127
Q

Hgb with 2 alpha and 2 delta chains

A

HbA2

128
Q

Comprises 2% of total adult Hgb

A

HbA2

129
Q

HbA1C forms when glucose enters RBC and glycates_____ residues and the amino terminals of Hgb

A

Epsilon amino group of lysine

130
Q

Based on ADA recommendations, cutoff of HbA1C for the diagnosis of diabetes is >/=____

A

6.5 %

131
Q

Lowering A1C to below ___% has been shown to reduce micrivascular and neuropathic complications of type 1 and type 2 DM

A

7

132
Q

Form of Hgb bound to carbon monoxide in place of oxygen

Hb becomes cherry pink in color

A

Carboxyhemoglobin

133
Q

CO has ___ times greater afficnitu for Hgb than oxygen

A

200

134
Q

Oxidized form of Hgb (Fe3+) that does nor bind oxygen as readily but has increased affinity for cyanide

A

Methemoglobin

135
Q

Chocolate cyanosis, O2 saturation is at 85%

Anxiety, headache, dyspnea

A

Methemoglobinemia

136
Q

Treatment for methemoglobinemia

A

Methylene blue or ascorbic acid (both reducing agents)

137
Q

Treatment for acute massive methemoglobinemia due to ingestion of chemicals

A

IV methylene blue

138
Q

Disorder characterized by an inherited defect in the RBC membrane that renders the erythrocytes spheroidal, less deformable , and vulnerable to splenic sequestration

A

Hereditary spherocytosis

139
Q

Mutation in what protein is most commonly implicated in hereditary spherocytosis

A

Ankyrin

Others:
Spectrin
Band 4.1
Band 3

140
Q

Diagnostic method for hereditary spherocytosis

A

Osmotic fragility test

141
Q

Treatment for symptomatic hereditary spherocytosis

A

Splenectomy

142
Q

Disease that results from point mutation in both genes coding for the beta chain that results to
Glutamine—>valine

A

Sickle cell dse

143
Q

Polymerization and decreased solubility of the deoxy form of Hb
Distortion of the RBC membrane
Misshapen, rigid RBCs that occlude capillaries

A

Sickle cell dse

144
Q

Anemia
Splenomegaly
Jaundice

A

Hereditary spherocytosis

145
Q

Anemia
Tissue anoxia
Painful crises
Protective against malaria

A

Sickle cell dse

146
Q

Treatment for sickle cell dse

A 
Hydration
Analgesics
Antibiotics if with infection
Transfusions
Hydroxyurea
147
Q

Hemoglobin variant that has a single amino acid substitution in 6th position of the beta globin chain, in which glutamate—->lysine

A

Hemoglobin C

148
Q

In hemoglobin C disease,

Glutamate —-> _____

A

Lysine

149
Q

T/F patients with Hgb C present with severe hemolytic anemia

A

F

Mild

150
Q

T/F

No specific therapy is required for Hgb C

A

T

151
Q

Inadequate synthesis of alpha chains
Anemia
Acumulation of Hb Bart (gamma 4) and Hb H (beta 4), and Beta chain precipitation

A

Alpha thalassemia

152
Q

In alpha thalassemia, symptoms appear at birth

T/F

A

T

because alpha chains are needed for HbF and HbA

153
Q

Silent carrier—>_____—>HbH disease —>Hydrops fetalis

A

Alpha thalassemia trait

154
Q

Inadequate synthesis of beta chains
Anemia
Accumulation if Hb Barts
And alpha chain precipitation

A

Beta thalassemia

155
Q

T/F symptoms of beta thalassemia appear only AFTER birth

A

T

156
Q

2 examples of fobrous proteins

A

Collagen

Elastin

157
Q

Most abundant protein in the body

A

Collagen

158
Q

Collagen structure is stabilized by ____ bonds

A

Hydrogen

159
Q

A long stiff extracellular structure in which 3 polypeptides (a chains) each 1000 AA in length are wound around ine another in a triple helix

A

Collagen

160
Q

Most common form of collagen

A

Type I

161
Q

Collagen is rich in what 2 AA

A

Proline

Glycine

162
Q

Facilitates kinking of the collagen structure

A

Proline

163
Q

Type of collagen found in BONE, skin, tendond, dentin, fascia, cornea, late wound repair

A

I

164
Q

Type of collagen found in CARTILAGE (including hyaline), vitreous body, nucleus pulposus

A

II

165
Q

Type of collagen found in RETICULIN, skin, blood vessels, uterus, fetal tissues, granulation tissue

A

III

166
Q

Type of collagen found in basemend membrane or basal lamina

A

Type IV

167
Q

Type of collagen beneath stratified squamous epithelium

A

Type 7

168
Q

Inherited disorder
Hyperextensibility of skin
Abnormal tissue fragility
Increased joint mobility

A

Ehlers Danlos Syndrome

169
Q 
Subtype of Ehlers Danlos
Defect in Type I and Type V collagen
Joint hypermobility
Severe skin abnormalities
Less severe joint changes
A

Classical

170
Q 
Subtype of Ehlers Danlos
Defect in Type III collagen
Joint hypermobility
Skin abn
Sever joint pain
Most common subtype
A

Hypermobility

171
Q

Ehlers Danlos Subtype
Type III
Fragile blood vessels and organs, small stature, thin and transluscent skin, easy bruising
Increased risk for intracranial aneurysms
Most serious

A

Vascular

172
Q

Multiple fractures
Blue sclerae
Hearinf loss
Dental imperfections

A

Osteogenesis imperfecta

173
Q

Most common form of osteogenesis imperfecta is autosomal _____ with abnormal collagen type ____

A

Dominant

Type I

174
Q

Main presenting sign of Alport syndrome

A

Hematuria

175
Q

Hematuria
Ocular lesions
Hearing loss
End stage renal dse

A

Alport syndrome

176
Q

Alport syndrome is defect in what type of collagen

A

IV

177
Q

Skin breaks and blisters

Defect in type VII collagen, which anchors the basal lamina to collagen fibrils in the dermis

A

Epidermolysis bullosa

178
Q

Sore spongy gums
Loose teeth
Poor wound healing
Petechiae on skin and mucous membrane

A

Scurvy

179
Q

Deficiency of this vitamin causes decreased cross linking of collagen fibers

A

Vitamin C

180
Q

Hydroxylation of collagen is a post-transcriptional modification requiring _______

A

Ascorbic acid

181
Q

Kinky hair and growth retardation

Dietary deficiency of copper required by lysyl oxidase

A

Menke’s disease

182
Q

Menkes dse reflects a dietary deficiency of copper required by _____

A

Lysyl oxidase

183
Q

Tissues that contain elastin

A 
Lungs
Large arteries
Elastic ligaments
Vocal cords
Ligamentum flavum
184
Q

______, precursor of elastin, is deposited into irregular fibrillin scaffold cross-linked by _____

A

Tropoelastin

Desmosine

185
Q

Marfan syndrome is caused by mutation by ______ gene

A

Fibrillin

186
Q 
Taller and thinner than family members
Dolichostenomelia
Arachnodactyly
Aortic dilatation and dissection
Upward dislocation of lens (ectopia lentis)
A

Marfan syndrome

187
Q

Airtic dilatation occurs in __ % of patients with Marfan syndrome

A

70-80

188
Q

Deficiency inhibits proteolytic enzymes from hydrolyzing and destroying proteins

A

Alpha 1 antitrypsin

189
Q 
Liver disease (cirrhosis and HCC)
Emphysema (due to alveolar wall destruction by elastase)
A

Alpha 1 antitrypsin deficiency

Biochemistry by mgcMD (19 decks)

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