1.Which factors are affecting electrophoresis mobilty?
a.molecule size
b. Shape of protine
c. a and b
d. none of the above
2. Which is not a type of zone electrophoresis ?
a.Gel electrophoresis
b.paper electrophoresis
c.Cellulose active electrophoresis
d. Micro electrophoresis
3. Which technique separates charged particles using electric field?
a. Hydrolysis
b. Electrophoresis
c. Protein synthesis
d. Protein denaturing
4. Which of the following statements is true about migration of biomolecules?
a. The rate of migration is directly proportional to the resistance of medium
b. Rate of migration is directly proportional to current
c. Low voltage is used for separation of high mass molecules
d. Rate of migration is inversely proportional to current
5. What does the electrophoresis apparatus consist of?
a. Gel, buffer chamber and fire pack
b. Buffer chamber and electrophoresis unit
c. Electrophoresis unit and gel separator
d. Power pack and electrophoresis unit
6. Which type of paper are used in paper electrophoresis?
a. whatman filter paper
b.cellulose acetate filter paper
c.chromatography paper
d. All of the above
7. what is agarose gel ?
a. Cross linkage molecules
b.Purified unchange poly saccharide
c.It is prepared by dissolving 0.5% agarose in boiling water and allowing it to cool to 40°C
d. All of the above
8.Which technique separates charged particles using electric field?
a) Hydrolysis
b) Electrophoresis
c) Protein synthesis
d) Protein denaturing
9.Electrophoresis was developed by:
a) Tswett
b) Tsvedberg
c) Tiselius
d) Sanger
10.The speed of migration of ions in electric field depends upon:
a) Shape and size of molecule
b) magnitude of charge and shape of molecule
c) Magnitude of charge shape and mass of molecule
d) Magnitude of charge and mass of molecule
11.Which of the following statements is true about migration of biomolecules?
a) The rate of migration is directly proportional to the resistance of medium
b) Rate of migration is directly proportional to current
c) Low voltage is used for separation of high mass molecules
d) Rate of migration is inversely proportional to current
12.What does the electrophoresis apparatus consist of?
a) Gel, buffer chamber and fire pack
b) Buffer chamber and electrophoresis unit
c) Electrophoresis unit and gel separator
d) Power pack and electrophoresis unit
13. . If proteins are separated according to their electrophoretic mobility then the type
of electrophoresis is:
a) SDS PAGE
b) Affinity Electrophoresis
c) Electro focusing
d) Free flow electrophoresis
14.The electrophoretic mobility denoted as µ is mathematically expressed as:
a) VE
b) E/V
c) 1/EV
d) V/E
15.Which of the following factors does not influence electrophoretic mobility?
a) Molecular weight
b) Shape of molecule
c) Size of molecule
d) Stereochemistry of molecule
16.When is electrophoresis not used?
a) Separation of proteins
b) Separation of amino acids
c) Separation of Lipids
d) Separation of nucleic acids
17.What cannot be a reason for using electrophoresis?
a) Comparing two sets of DNA
b) Organizing DNA by shape of backbone
c) Organizing DNA fragments from largest to smallest
d) Organizing DNA in order we can see
18. Which technique separates charged particles using electric field?
A Hydrolysis
B Electrophoresis
C Protein synthesis
D Protein denaturing
19.Agarose can be extracted from which of the following?
A Lycazusican esculentum
B Ficum benghalensis
C Gracilaria esculentus
D Agrostis stolonifera
20.The polymerization of the gel used in PAGE occurs between polyacrylamide and ____________
A N, N – acrylamide
B Bisacrylamide
C N – methyleneacrylamide
D N, N – methylene bisacrylamide
21.The fluorescent dye such Ethidium is used for visualizing DNA. How do ethidium binds to DNA?
A Stacked between histone molecules
B Binds to the nucleotide base
C Intercalated between the stacked bases
D Binds to the phosphodiester backbone
22.Pulse field gel electrophoresis separates DNA molecules of size ___________
A 10 – 20 bp
B 20 – 30 Kb
C 30 – 50 Kb
D 40 – 50 bp
23.Pulse field gel electrophoresis was developed by ____________
A Collins and John
B Kary Mullis
C Patrick O’ Farrell
D Schwartz and Cantor
24.For the separation of DNA by electrophoresis, which of the following method is commonly used?
A Agarose – vertical
B Agarose – horizontal
C PAGE – vertical
D PAGE – horizontal
25.Sodium dodecyl sulfate (SDS) used in SDS PAGE is___________.
A An anionic detergent
B A cationic detergent
C A non-ionic detergent
D An anion exchanger
26.In SDS-PAGE, migration of protein is effected by ____________.
A Charge of protein
B Size of protein
C Net charge of protein
D All of these
27.The main advantage of discontinuous buffer system in SDS and Native PAGE is ________.
A Conformation of protein is conserved
B Constantly maintain the charge of proteins
C Assist in migration of protein
D Enhance resolution of separation
28.The role of APS in SDS PAGE is to________.
A Act as a catalyst in the polymerization of acrylamide
B Act as a source of free radicals
C Act as a bridge between acrylamide and bis-acrylamide
D Act as a pore builder in the polymerized gel
29.Which of the following is used as a ‘tracking dye’ in SDS-PAGE of protein?
A Bromophenol blue
B Xylene cyanol
C Orange G
D All of these
30.For the better resolution of minute protein bands in SDS-PAGE, which of the following staining
method is advised?
A CBB Staining
B Silver staining
C Avidin staining
D All of these
31.In a gel filtration column
A smaller proteins enter the beads more readily
B large proteins elute first
C both (1) and (2)
D large proteins enter the beads more readily
32.In isoelectric focusing, proteins are separated on the basis of their
A relative content of positively charged residue only
B relative content of negatively charged residue only
C size
D relative content of positively and negatively charged residue
33.In SDS-PAGE, the protein sample is first
A treated with a reducing agent and then with anionic detergent followed by fractionation by
electrophoresis
B fractionated by electrophoresis then treated with an oxidizing agent followed by anionic detergent
C treated with a oxidizing agent and then with anionic detergent followed by fractionation by
electrophoresis
D none of the above
34.In an SDS-PAGE
A proteins are denatured by the SDS
B proteins have the same charge-to-mass ratio
C smaller proteins migrate more rapidly through the gel
D all of the above
35.In a native PAGE, proteins are separated on the basis of
A net negative charge
B net charge and size
C net positive charges size
D net positive charge
36.The role of urea in PAGE separation of DNA is to _______.
A Act as anion
B Act as cation
C Helps to denature the DNA
D Provide buffer stability of the gel
37.In native-PAGE the separation of protein is influenced by ___________.
A Charge of protein
B Size of protein
C pI of protein
D Both (a) and (b)
38.In electrophoresis, the electrophoretic mobility (‘µ’) is determines the characteristics of migration of
different biomolecules. Which of the following is not having any influence in ‘µ’?
A Size of molecule
B Shape of molecule
C Molecular weight
D Stereochemistry of molecule
39.Function of β-mercaptoethanol in SDS-PAGE is__________.
A To give negative charges to amino acids in the proteins
B For the oxidation of disulfide bonds in the proteins
C For breaking hydrogen bonds in the proteins
D For the reduction of disulfide bonds in the proteins
40.In SDS-PAGE of protein separation, one SDS molecule will binds to __________.
A Every amino acid
B Every two amino acids
C Every three amino acids
D Every Four amino acids
