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Biomolecules > Proteins PPT > Flashcards

Proteins PPT Flashcards

1
Q

during denaturation, proteins will not lose their structure, with regard to

A

primary structure

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2
Q

the characteristic features of the peptide bond include all the following, except

a. does not allow freedom of rotation
it is a partial double bond
always has cis configuration
absorbs UV light at 280 nm

A

always has cis configuration

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3
Q

the force maintaining the primary structure of a protein:

A

peptide bond

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4
Q

The forces maintaining the secondary, tertiary and quaternary structures of a protein are the follow-ing, except:

A. Electrostatic (ionic) bonds
B. Hydrophobic forces
C. Van der Waals forces
D. Peptide bond

A

peptide bond

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5
Q

The amino acid which did not allow formation of alpha-helix is

A

Proline

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6
Q

Tertiary structure of a protein describes

A. The sequence of amino acids B. Location of disulphide bonds
C. Amino terminal end amino acid D. The nature of protein folding

A

nature of protein foldng

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7
Q

One of the following proteins does not have a qua-ternary structure:

A. Albumin
B. Hemoglobin
C. Lactate dehydrogenase
D. Immunoglobulin G

A

albumin

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8
Q

All the following reagents are used for identifying the rst amino acid in a protein, except:

A. Cyanogen bromide
B. Fluorodinitrobenzene
C. Dansyl chloride
D. Phenyl isothiocyanate

A

cyanogen bromide

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9
Q

Proteins can be precipitated by the following meth-ods, except:

A. Adding alcohol and acetone
B. Saturating with ammonium sulphate
C. Using salts of heavy metals
D. Shifting the pH away from the iso electric point

A

D. Shifting the pH away from the iso electric point

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10
Q

Denatured proteins:

A. Are soluble
B. Are difcult to digest
C. Are biologically inactive
D. Peptide bonds are broken

A

C. Are biologically inactive

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11
Q

Which of the following is a simple protein?

A. Casein
B. Insulin
C. Hemoglobin
D. Tyrosinase

A

Insulin

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12
Q

In glycoproteins, the carbohydrate chains are com-bined through glycosidic linkages with:

A. Hydroxyl groups of serine or threonine residues of proteins
B. Epsilon amino nitrogen of lysine residues of pro-teins
C. Guanidium group of arginine residues of proteins
D. Phenol group of tyrosine residues of proteins

A

A. Hydroxyl groups of serine or threonine residues of proteins

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13
Q

The protein which does not answer the aldehyde test is

A

Gelatin

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14
Q

Proteins may be estimated by the following meth-ods, except

A. Biuret method
B. Heat coagulation
C. Kjeldahl’s digestion
D. Nephelometry

A

B. Heat coagulation

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15
Q

All the following are examples of tertiary structure of proteins, except:

A. Alpha helix
B. Beta pleated sheet
C. Triple stranded helix
D. Peptide bonds

A

Peptide bonds

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16
Q

Tertiary structure of a protein describes

A

D. The nature of protein folding

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17
Q

4-17. Proteins may be denatured irreversibly by:

A. Adding urea
B. Bringing to iso electric pH
C. Heat coagulation
D. Reduction with mercaptoethano

A

C. Heat coagulation

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18
Q

Lectins are:

A. Animal proteins having specic amino acid binding site
B. Antibody molecules acting against cells
C. Plant proteins having specic carbohydrate bind-ing site
D. Blood proteins having a lecithin group

A

D. Blood proteins having a lecithin group

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19
Q

Ultraviolet light at 280 nm is absorbed by which component of proteins?

A. Peptide bonds
B. Sulfhydryl group of cysteine
C. Indole ring of tryptophan
D. Imidazole ring of proline

A

Indole ring of tryptophan

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20
Q

The nature of the bond linking amino acids to each other is

A. Covalent
B. Co-ordinate
C. Ionic
D. Hydrophobic

A

covalent

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21
Q

How many peptide bonds are present in gluta th-ione?

A. 1 B. 2 C. 3 D. 4

A

c. 3

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22
Q

Basic difference between two polypeptides is in the —

A. Structural conformation
B. Primary sequence of amino acids C. Number of side chains
D. Number of hydrophobic bonds

A

B. Primary sequence of amino acids

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23
Q

Human insulin differs from bovine insulin in:

A. Biological activity
B. Number of amino acids
C. Position of disulde bonds
D. Sequence of amino acids

A

D. Sequence of amino acids

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24
Q

A covalent bond between the alpha carboxyl group of one amino acid and alpha amino group of the neighboring amino acid is called

A. Cis double bond
B. Isopeptide bond
C. Pseudopeptide bond
D. Peptide bond

A

peptide bond

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25
Q

Study of linear sequence of amino acids is done by all techniques listed except:
A. End group analysis
B. Hydrolysis by proteolytic enzymes
C. Analyzing the content of each amino acid
D. Denaturing the protein

A

D. Denaturing the protein

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26
Q

Different polypeptide chains are held together by:

A. Peptide bonds
B. Disulphide bonds
C. Glycosidic bonds
D. Ester bonds

A

B. Disulphide bonds

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27
Q

Primary structure decides:

A. Rate of synthesis of protein
B. Biological activity of the protein C. Rate of degradation of the protein
D. Effect of proteolytic enzymes on protein

A

B. Biological activity of the protein

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28
Q

Secondary and tertiary levels of protein structure are dependent on

a. Presence of disulde bonds
b. Primary structure
c. PH of the medium
d. PK value of component amino acids

A

b. Primary structure

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29
Q

The protein having predominantly alpha heli cal structure is

collagen
keratin
fibroin
myoglobin

A

collagen

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30
Q

Which of the following is NOT true regarding the tertiary structure of proteins

A. It is a random coil structure
B. Disulde bonds are formed between any two cys-teine residues C. Position of disulde bonds are predetermined and xed
D. Denaturation using reducing agents does not aff-ect the disulde bonds

A

D. Denaturation using reducing agents does not aff-ect the disulde bonds

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31
Q

Protein having a large number of disulde bonds is

A. collagen B. keratin C. hemoglobin D. albumin

A

keratin

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32
Q

Which of the following proteins does not possess a quaternary structure?

A. Myoglobin
B. Lactate dehydrogenase
C. Hemoglobin
D. Immunoglobulin M

A

A. Myoglobin

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33
Q

Which of the following is NOT true regarding hem-oglobin?

A. Has 4 independent subunits
B. Each subunit has one heme residue
C. Each subunit can bind one molecule of oxygen
D. All four subunits are similar

A

D. All four subunits are similar

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34
Q

draw glycine structure

A

+1

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35
Q

draw Alanine structure

A

+1

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35
Q

glycine letter code

A

Gly/G

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36
Q

glycine is

polar
nonpolar
+ charge
- charge

A

non-polar

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37
Q

Alanine is?

polar
nonpolar
+ charge
- charge

A

non-polar

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38
Q

alanine letter code

A

Ala/A

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39
Q

draw valine structure

A

+1

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40
Q

valine is ?

polar
nonpolar
+ charge
- charge

A

non polar

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41
Q

draw cysteine structure +1

A

+1

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42
Q

cysteine is

polar
nonpolar
+ charge
- charge

A

non polar

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43
Q

cysteine letter code

A

Cys/C

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44
Q

valine letter code

A

Val/V

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45
Q

Proline letter code

A

Pro/P

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46
Q

draw proline structure

A

+1

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47
Q

proline is

polar
nonpolar
+ charge
- charge

A

nonpolar

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48
Q

draw leucine structure

A

+1

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49
Q

leucine is

polar
nonpolar
+ charge
- charge

A

non polar

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50
Q

leucine letter code

A

Leu L

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51
Q

draw isoleucine structure

A

+1

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52
Q

isoleucine is

polar
nonpolar
+ charge
- charge

A

nonpolar

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53
Q

isoleucine letter code

A

Ile / I

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54
Q

methionine structure

A

+1

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55
Q

methionine is

polar
nonpolar
+ charge
- charge

A

nonpolar

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56
Q

methionine letter code

A

Met/M

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57
Q

Tryptophan structure

A

+1

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58
Q

Tryptophan is

polar
nonpolar
+ charge
- charge

A

nonpolar

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59
Q

Tryptophan letter code

A

Trp/W

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60
Q

Phenylalanine structure

A

+1

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61
Q

Phenylalanine is

polar
nonpolar
+ charge
- charge

A

nonpolar

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62
Q

Phenylalanine letter code

A

Phe/F

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63
Q

Lysine structure

A

+1

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64
Q

Lysine is

polar
nonpolar
+ charge
- charge

A

+ charge

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65
Q

Lysine letter code

A

Lys/K

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66
Q

Arginine structure

A

+1

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67
Q

Arginine is

polar
nonpolar
+ charge
- charge

A

+ charge

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68
Q

Arginine letter code

A

Arg/R

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69
Q

Histidine structure

A

+1

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70
Q

Histidine is

polar
nonpolar
+ charge
- charge

A

+ charge

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71
Q

Histidine letter code

A

His/H

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72
Q

serine structure

A

+1

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73
Q

serine is

polar
nonpolar
+ charge
- charge

A

polar

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74
Q

serine letter word

A

Ser/S

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75
Q

Threonine structure

A

+1

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76
Q

Threonine structure

A

+1

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77
Q

Threonine is

polar
nonpolar
+ charge
- charge

A

polar

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78
Q

Tyrosine structure

A

+1

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79
Q

Threonine letter code

A

Thr/T

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80
Q

Tyrosine letter code

A

Tyr/Y

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81
Q

Tyrosine structure

A

+1

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82
Q

Tyrosine is

polar
nonpolar
+ charge
- charge

A

polar

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83
Q

Asparagine structuer

A

+1

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84
Q

Asparagine

polar
nonpolar
+ charge
- charge

A

polar

85
Q

Asparagine letter code

A

Asn/N

86
Q

Glutamine structure

A

+1

87
Q

Glutamine is

polar
nonpolar
+ charge
- charge

A

polar

88
Q

glutamine letter code

A

Gln/Q

89
Q

Aspartic acid structure

A

+1

90
Q

Aspartic acid is

polar
nonpolar
+ charge
- charge

A
  • charge
91
Q

aspartic acid letter code

A

Asp/D

92
Q

Glutamic acid structure

A

+1

93
Q

Glutamic acid is

polar
nonpolar
+ charge
- charge

A
  • charge
94
Q

Glutamic acid letter code

A

Glu/ E

95
Q

Amino acids with aliphatic side chains (5)

A

Glycine (G), Alanine (A), Valine (V), Leucine (L) and Isoleucine (I)

96
Q

amino acids that have branched amino acid chains

A

Valine
Leucine
Isoleucine

97
Q

Hydroxyl group containing amino acids (3)

A

Serine (S)
Threonine (T)
Tyrosine (Y)

98
Q
  1. Sulphur containing amino acids (2)
A

Cysteine
Methionine

99
Q

is formed by the condensation of two cysteine molecules.

A

Cystine

100
Q
  1. Acidic amino acids and their amides (4)
A

Glutamic acid (E) and Aspartic acid (D)
Glutamine (Q) and Asparagine (N) are their respective amide derivatives.

101
Q

Basic amino acids:

A

Lysine (K), Arginine (R) (with guanidine group) and Histidine (H)(with imidazole ring

102
Q
  1. Aromatic amino acids (3)
A

Phenylalanine (F), Tyrosine (Y) and Tryptophan (w) (with indole ring)

103
Q

Imino acids

A

Proline

104
Q

ionic forms of the amino acid (neutral = net charge 0)

A

zwitterion

105
Q

amino acids that show optical and stereochemical properties

A

asymmetric/chiral carbon

106
Q

only achiral carbon

A

glycine

107
Q

same chemical composition, different spatial organization

A

stereoisomers

108
Q

type of stereoisomers where nonsuperimposable mirror-image (L and D)

A

enantiomers

109
Q

L means

A

Levorotatory behaviour

110
Q

D means

A

Dextrorotatory

111
Q

types of amino acids that predominate in nature

A

L-amino acids

112
Q

are amino acids weak/strong polyprotic acids

A

weak

113
Q

An acid that contains more than one ionizable proton

A

polyprotic acid

114
Q

pH where amino acids have a net charge of 0

A

isoeletric point (pI)

115
Q

pI formula

A

1/2 (pK1+pK2)

116
Q

at neutral pH, acidic amino acids have a what net charge

A

negative

117
Q

acidic amino acids pI formula

A

pI = 1/2 (Pk1+PKr)

118
Q

have net positive charge at neutral pH

A

basic amino acids

119
Q

pI for basic amino acids

A

pI = 1/2 (Pkr+PK2)

120
Q

produced by modifications of one of the 20 amino acids already incorporated into a protein

A

uncommon amino acids

121
Q

example of uncommon amino acids

A

carboxyglutamate
hydroxyproline
hydroxylysine
selenocysteine
phosphoserine

122
Q

example uncommon amino acids with biological functions (occur rarely in proteins)

A

dopamine
histamine
citrulline
GABA
Tiroxine
L-ornithine

123
Q

neurotransmitter

A

dopamine

124
Q

allergy reactions

A

histamine

125
Q

urea cycle intermediate (2)

A

Citrulline
L-ornithine

126
Q

covalent amide bond established between a-COOH and a-NH3+ groups of two amino acids

A

peptide bond

127
Q

allow the polymerisation of amino acids to form peptides and proteins

A

polymerisation

128
Q

usually found in trans conformation

A

peptide bond

129
Q

about 0.133nm long (shorter than single bond butl onger than a double bond))

A

peptide bond

130
Q

peptides according to number of amino acids

A

dipeptide
tripeptide
oligopeptide
polypeptide

131
Q

more than 12 but less than 20 amino acids

A

oligopeptide

132
Q

liberates the amino acids of a protein

A

acid hydrolysis

133
Q

chromatographic methods used to separate amino acids:

A

ion exhcange chromatography
thin layer chromatography
reverse-phase high performance liquid chromatography (HPLC)

134
Q

the charged molecule of interest are exchanged for another ion (salt ion) on a charged solid support (resins)

A

ion exchange chromatography

135
Q

amino acids absorbed on a thin layer of silica gel

A

thin layer chromatography

136
Q

amino acids separated on the based of their polarity by the use of a column having a nonpolar liquid immobilised on an inert matrix

A

HPLC

137
Q

reagent that combines with free amino terminus of protein

A

Phenylisothiocynate

138
Q

not only identifies the N-terminal residue of protein, successive reaction cycles can reveal the amino acid sequence of a peptide

A

flourescence

139
Q

proteins for catalysis

A

enzymes

140
Q

proteins for structural role

A

collagen
fibroin
elastn

141
Q

proteins against mechanical or chemical damage

A

keratin

142
Q

proteins to avoid blood loss

A

fibrinogen and thrombin

143
Q

proteins for immunosystem proteins

A

immuoglobins

144
Q

proteins for storage

A

ovalbumin
casein
ferritin

145
Q

protein without prosthetic group

A

apoprotein

146
Q

protein with prostetic group

A

holoprotein

147
Q

overall three dimesional architecture of aprotein (the radicals can be modified their spatial position by rotation, bonds are not cleavage during this process)

A

conformation

148
Q

geometric possibilities from a particular set of atoms. In going from one configuration from another, covalent bonds must be broken and rearranged

A

configuration

149
Q

strands run in opposite directions

A

antiparallel

150
Q

usually located in the protein surface
stabilized by hydrogen bonds
they allow the protein strands to change direction
glycine and proline are predominant amino acids

A

beta-turns

151
Q

combinations of few secondary strtuctures giving characteristic geometric shape

A

supersecondary strctures

152
Q

globular proteins containing a combination of different super secondary structures

A

domains or modules

153
Q

location of amino acids side chain in globular proteins are based on polarities

nonpolar are (inside/outside)

A

inside

154
Q

location of amino acids side chain in globular proteins are based on polarities

charged are usually located at what

A

surface of protein

155
Q

location of amino acids side chain in globular proteins are based on polarities

polar and uncharged are located

A

inside the protein/in the surface (usually)

156
Q

interactions allowing tertiary structure stabilization

A

charge-charge
van der Waals repulsion
hydrogen bonds
hydrophobic interactions
disulfide bridges

157
Q

loss of protein structure and function

A

denaturation

158
Q

restoration of native structure and biological role

A

renaturation

159
Q

proteins that may assist the protein folding process

A

chaperones

160
Q

condensed intermediate on the folding pathway that contains much of the secondary structure elements on the native conformation but many incorrect tertiary structure interactions

A

molten-globule

161
Q

protein containing several identical subunits

A

oligomer

162
Q

structural unit of an oligomeric protein

A

protomer

163
Q

contains two protomers

A

tetramers

164
Q

found in epidermal layer, nails, hair, feathers

A

fibrous proteins (a-keratins)

165
Q

different grade of hardness of a-keratin is on the basis of what residue

A

%CYs disulfide bridges

166
Q

most abundant protein in vertebrates

A

colalgen

167
Q

provides framework that gives the tissues their form and strength

A

collagens

168
Q

simple helical structure (left handed)

A

collagen

169
Q

inorganic form of collagen

A

hydroxyapatite

170
Q

method that is titration based, measure nitrogen then protein are detected

A

Kjeldahl method

171
Q

high temperature is required for this

A

Enhanced dumas method

172
Q

when high conc. of protein is present

A

Biureate test

173
Q

low conc. of protein present unable to detect through Biureate

A

lowery methods

174
Q

biurate reagent + phosphomolybdate and phosphotungstate

A

lowery method

175
Q

solubility testare tests performed to determine the ability of compounds to dissolve in a solvent, which is usually a liquid. These tests are essential to determine the size and polarity of unknown compounds and the presence of acidic and basic functional groups.

A

solubility test

176
Q

protein is not soluble in solvent looks like

A

cloudy solution

177
Q

a chemical test useful to identify ammonia, primary/secondary amines, or amino acid

A

ninhydrin test

178
Q

positive for ninhydrin test

A

purple-colored complex

179
Q

proline in ninhydrin test

A

yellow

180
Q

is a chemical test which is used to check whether a given analyte contains amines or α-amino acids.

A

ninhydrin test

181
Q

positive in ninhydrin test indicates

A

presence of ammonia, primary/secondary amines, or amino acids

182
Q

a chemical test that can be used to check for the presence of peptide bonds in a given analyte.

A

biuret test

183
Q

biuret reagent

A

hydrated copper sulfate
sodium hydroxide
sodium-potassium tartate

184
Q

pink in biuret test indicates

A

presence of peptides

185
Q

is used to detect amino acids containing an aromatic nucleus (tyrosine, tryptophan and phenylalanine) in a protein solution which gives yellow color nitro derivatives on heating with conc. HNO3.

A

xanthoproteic test

186
Q

reagent for xanthoproteic test

A

conc. nitric acid
40% NaOH

187
Q

xanthoproteic test positive indicates

A

tyrosine and tryptophan present

188
Q

color of positive xanthoproteic test

A

yellow
orange

189
Q

is an analytical test used for the detection of the amino acid tyrosine, which is the only amino acid containing the phenol group.

A

Millon’s test

190
Q

millon’s reagent

A

mercuric nitrate
mercurous nitrate
in nitric acid and distilled water.

191
Q

Millon’s reagent positive is indicated by

A

red or pink precipitate present

192
Q

is a time-tested colorimetric assay.

A

Bradford assay

193
Q

is a widely used colorimetric method for determining protein concentration in a solution

A

bradford assay

194
Q

reagent in Bradford assaywhich is prepared in phosphoric acid. When the dye binds to proteins, it undergoes a color change that shifts the absorbance maximum from 465 nm to 595 nm

A

Coomassie Brilliant Blue G-250

195
Q

the intensity of the color change is directly/indirectly proportional to the protein concentration,

A

directly

196
Q

is a biochemical test consisting of colorimetric reaction for the detection and quantification of guanidinium groups, used as a qualitative test for arginine that is either free or in protein

A

sakaguchi test

197
Q

sakaguchi reagent

A

1% 1-naphthol in alcohol with a few drops of 10% sodium hypobromite solution of bromine water.

198
Q

sakaguchi positive test indicates

A

presence of arginine or guanidium compound

199
Q

color of positive sakaguchi test

A

red

200
Q

is a specific test used for the detection of indole ring and thus, tryptophan in proteins.

A

hopkin’s cole test

201
Q

hopkin’s cole reagent

A

Glyoxylic acid

202
Q

positive hopkin’s cole is indicated by

A

purple ring

203
Q

positive hopkin’s cole test means

A

tryptophan is present

204
Q

looks for the presence of cystine in the urine through a semi-quantitative test

A

nitroprusside test

205
Q

s a biochemical test used for the detection of the free –SH groups in amino acids or the cysteine amino acid in a protein.

A

nitroprusside test

206
Q

reagent for nitruprusside test

A

2 freshly prepared sodium nitroprusside
Concentrated Sodium hydroxide

207
Q

positive nitroprusside test indicator

A

red colored complex

208
Q

positive nitroprusside test means

A

cysteine is present

209
Q

view ppt

A

+1

Biomolecules (23 decks)

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