Multiple Choice Questions on Electrophoresis

1. The technique electrophoresis, for the separation of charged molecules was developed by

a) Tswett

b) Svedberg

c) Tiselius

d) Sanger

2. In electrophoresis, DNA will migrate towards

a) cathode or positive electrode

b) anode or negative electrode

c) cathode or negative electrode

d) anode or positive electrode

3. The speed of migration of ions in an electric field depends on

a) magnitude of charge and mass of molecules

b) magnitude of charge and shape of molecules

c) shape and size of the molecule

d) magnitude of charge, shape and mass of molecules

4. Which of the following statement is true regarding migration of bio molecules?

a) the rate of migration is directly proportional to the current

b) the rate of migration is inversely proportional to current

c) the rate of migration is directly proportional to the resistance of the medium

d) Low voltage is used for the separation of high molecular weight compounds
5. Electrophoresis cell or electrophoresis apparatus consists of

a) power pack and electrophoresis unit

b) Elctrophoresis unit and DNA separator

c) buffer chamber and Elctrophoresis unit

d) Gel, buffer chamber and power pack

6. The most common type of gel used for DNA separation is

a) Agar

b) Polyacrylamide

c) Agarose

d) All of the above

7. Which is the technique suited for the separation of large DNA fragments

a) AGE

b) PAGE

c) PFGE

d) SDS-PAGE

8. What is the role of SDS in SDS-PAGE?

a) protein denaturing and imparting net negative charge

b) imparting overall negative charge to the protein

c) imparting equal mass to all proteins

d) protein unfolding and imparting net positive charge

9. In SDS-PAGE, separation is based on

a) molecular weight

b) shape

c) charge

d) all of the above

10. The electrophoresis technique that used isoelectric focusing is

a) AGE

b) PFGE

c) 2D-PAGE

d) SDS-PAGE

Which of the following is not a common support medium used in electrophoresis techniques:

a. Cellulose acetate

b. Agarose gel

c. Polyacrylamide gel

d. Dextrose

In agarose gel electrophoresis, DNA is moved towards the

a. cathode
b. anode
c. DNA doesn't move
d. none of above

MCQ. In SDS electrophoresis, proteins are separated on basis of

a. charge
b. mass
c. both A and B
d. structure

MCQ. If proteins are separated according to their electrophoretic mobility then type of electrophoresis
is

a. SDS page
b. free flow electrophoresis
c. electro focusing
d. affinity electrophoresis

MCQ. A technique which separates charged particles using electric field is

a. Hydrolysis
b. electrophoresis
c. protein synthesis
d. protein denaturing
3) 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

4). Sodium dodecyl sulfate (SDS) used in SDS PAGE is___________.

a. An anionic detergent

b. A cationic detergent

c. A nonionic detergent

d. An anion exchanger

e. A cation exchanger

5). Function of βmercaptoethanol in SDSPAGE is__________.

a. To give negative charges to amino acids in the proteins

b. For the oxidation of disulfide bonds in the proteins

c. For the reduction of disulfide bonds in the proteins

d. For breaking hydrogen bonds in the proteins

7). 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. Stereochemistry of molecule

b. Size of molecule

c. Shape of molecule

d. Molecular weight

e. Net charge of molecule

8). Electrophoresis is not used for the separation of ________.

a. Nucleic acids

b. Proteins

c. Amino acids

d. Lipids

9). In SDSPAGE 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

10). In SDSPAGE, migration of protein is effected by ____________.

a. Charge of protein

b. Size of protein

c. Net charge of protein

d. All of these

11). InnativePAGE the separation of protein is influenced by ___________.

a. Charge of protein

b. Size of protein

c. pI of protein

d. Both (a) and (b)

e. Both (b) and (c)

12). 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

13). The pH of (i) stacking, (ii) resolving gel and (iii) tank buffer in SDS PAGE is

_________ respectively.

a. (i). 8.30 (ii) 8.80 (iii) 6.80

b. (i). 6.80 (ii) 8.80 (iii) 8.30

c. (i). 8.30 (ii) 6.80 (iii) 8.80

d. (i). 6.80 (ii) 8.30 (iii) 8.80

14). The percentage of SDS commonly used in the buffers of SDS PAGE is

__________.

a. 0.1 %

b. 1.0 %

c. 10 %

d. 1 – 10 %

15). 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

16). 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 bisacrylamide

d. Act as a pore builder in the polymerized gel

17). The ‘tracking dye’ used in SDS PAGE will be ______.

a. Anionic

b. Cationic

c. Nonionic

d. Amphipathic

18). Which of the following is used as a ‘tracking dye’ in SDSPAGE of protein?

a. Bromophenol blue

b. Xylene cyanol

c. Orange G

d. Both (a) and (b)

e. All of these

19). Glycerol is added to protein samples before they are loaded to the ‘wells’ of

PAGE. The function of glycerol is to _______.

a. Stabilize protein structure

b. Provide density to the sample

c. Helps to bind SDS to the protein

d. Helps to reduce disulfide bonds by βmercaptoethanol

20). For the better resolution of minute protein bands in SDSPAGE, which of

the following staining method is advised?

a. CBB Staining

b. Silver staining

c. Avidin staining

d. All of these
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

Proteins can be visualized directly in gels by

A. staining them with the dye

B. using electron microscope only

C. measuring their molecular weight

D. none of these

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

Electrophoresis of histones and myoglobin under non-denaturing conditions (pH = 7.0) results in

A. both proteins migrate to the anode

B. histones migrate to the anode and myoglobin migrates to the cathode

C. histones migrate to the cathode and myoglobin migrates to the anode

D. both proteins migrate to the cathode

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

Flow cytomertery

Which part of the cytometer consists of the excitation sources and detectors?
a) .Optics
b) .Electronics
c) Fluidics

What does light emitted as side scatter (SSC) measure?

A.Cell size
B.Cell granularity / complexity
C.Cell surface marker fluorescence
 
Which part of the cytometer converts the light signal to voltage so it can be
interpreted through a computer software?
A.Fluidics
B.Optics
C.Electronics
 

What does light emitted as foward side scatter (FSC) measure?

A.Cell size
B.Cell granularity / complexity
C.Cell surface marker fluorescence