Gel Retardation Technique MCQs most propably ask in CSIR NET Exam.


 Hello friends, in today's article we see the gel retardation technique MCQs in genetic engineering. In this, we see the electrophoresis MCQs, SDS page, PFGE, PAGE, etc

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Gel Retardation Technique MCQs most propably ask in CSIR NET Exam.


Gel Retardation Technique MCQs:-




Gel Retardation Technique MCQs:-


1. Which technique separates charged particles using an electric field?

a) Hydrolysis

b) Electrophoresis

c) Protein synthesis

d) Protein denaturing



2. Electrophoresis was developed by:

a) Tswett

b) Tsvedberg

c) Tiselius

d) Sanger




3. The speed of migration of ions in the electric field depends upon:

a) Shape and size of the molecule

b) Magnitude of charge and shape of the molecule

c) Magnitude of charge shape and mass of the molecule

d) Magnitude of charge and mass of the molecule



4. Which of the following statements is true about the migration of biomolecules?

a) The rate of migration is directly proportional to the resistance of the 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) Powerpack and electrophoresis unit




6. 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



7. The electrophoretic mobility denoted as µ is mathematically expressed as:

a) VE

b) E/V

c) 1/EV

d) V/E




8. Which of the following factors does not influence electrophoretic mobility?

a) Molecular weight

b) Shape of the molecule

c) Size of molecule

d) Stereochemistry of molecule




9. When is electrophoresis not used?

a) Separation of proteins

b) Separation of amino acids

c) Separation of Lipids

d) Separation of nucleic acids




10. What cannot be a reason for using electrophoresis?

a) Comparing two sets of DNA

b) Organizing DNA by the shape of the backbone

c) Organizing DNA fragments from largest to smallest

d) Organizing DNA in order we can see



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

  1. Tswett

  2. Svedberg

  3. Tiselius

  4. Sanger




12. In Electrophoresis, DNA will migrate towards

  1. The cathode or positive electrode

  2. The anode or negative electrode

  3. The cathode or negative electrode

  4. The anode or positive electrode




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

  1. The magnitude of charge and mass of molecules

  2. The magnitude of charge and shape of molecules

  3. Shape and size of molecules

  4. The magnitude of charge, shape, and mass of molecules



14. Which of the following statements is true regarding the migration of biomolecules?

  1. The rate of migration is directly proportional to the current

  2. The rate of migration is inversely proportional to the current

  3. The rate of migration is directly proportional to the resistance of the medium

  4. Low voltage is used for the separation of high molecular weight compounds



15. Elcetroporesis gel or electrophoresis apparatus consists of 

  1. Powerpack and electrophoresis unit

  2. Electrophoresis unit and DNA separator

  3. Buffer chamber and electrophoresis unit

  4. Gel, buffer chamber, and power pack



 

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

  1. Agar

  2. Polyacrylamide

  3. Agarose

  4. All of these



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

  1. AGE

  2. PAGE

  3. PFGE

  4. SDS-PAGE




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

  1. Protein denaturing and imparting a net negative charge 

  2. Imparting overall negative charge to the protein

  3. Imparting equal mass to all proteins

  4. Protein unfolding and imparting a net positive charge




19. In SDS-PAGE, separation is based on 

  1. Molecular weight

  2. Shape 

  3. Charge

  4. All of the above



20. The electrophoresis technique that used isoelectric focusing is 

  1. AGE

  2. PFGE 

  3. 2D-PAGE

  4. SDS-PAGE




21. In an SDS-PAGE

  1. Proteins are denatured by the SDS

  2. Protein has the same charge-to-mass ratio

  3. Smaller proteins migrate through the gel

  4. All of the above



22. Protein can be visualized directly in gels by 

  1. Staining them with the dye 

  2. Using electron microscope only

  3. Measuring their molecular weight

  4. None of these



23. In SDS-PAGE, the protein sample is first

  1. Treated with a reducing agent and then with anionic detergent followed by fractional by electrophoresis

  2. Fractionated by electrophoresis then treated with an oxidizing agent followed by anionic detergent.

  3. Treated with an oxidizing agent and then with anionic detergent followed by fractionation by electrophoresis

  4.  None of the above




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

  1. Both proteins migrate to the anode 

  2. Histones migrate to the anode and myoglobin migrate to the cathode

  3. Histones migrate to the cathode and myoglobin migrate to the anode

  4. Both proteins migrate towards the cathode




25. In isoelectric focusing, proteins are separated on the basis of their 

  1. The relative content of positively charged residue only

  2. The relative content of negatively charged residue only

  3. Size

  4. The relative content of positively and negatively charged residue



26. In a gel filtration column

  1. Smaller proteins enter the beads more readily

  2. Large proteins elute first

  3. Both a and b

  4. Large proteins enter the beads more readily



27. In a native PAGE, proteins are separated on the basis of 

  1. Net negative charge

  2. Net positive charge

  3. Net positive charges size

  4. Net positive charge




28. The submission of molecular weight, as well as the number of subunits in the quaternary structure, can be determined by 

  1. SDS-PAGE electrophoresis

  2. Gel filtration chromatography

  3. Combining information from a and b

  4. Isoelectric focusing



29. Proteins are separated in an SDS-PAGE experiment on the basis of their 

  1. Positively charged side chains

  2. Molecular weight

  3. Negatively charged side chains

  4. Different isoelectric point



30. Which factors are affecting electrophoresis mobility?


a) molecule size

b) Shape of protein

c)  a and b

d) none of the above



31. Which is not a type of zone electrophoresis?


a) Gel electrophoresis

b) paper electrophoresis

c) Cellulose active  electrophoresis

d) Micro electrophoresis



32. Which technique separates charged particles using an electric field?

a) Hydrolysis

b) Electrophoresis

c) Protein synthesis

d) Protein denaturing



33. Which of the following statements is true about the migration of biomolecules?

a) The rate of migration is directly proportional to the resistance of the 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



34. 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) Powerpack and electrophoresis unit



35. Which type of paper is used in paper electrophoresis?


a) Whatman filter paper

b) cellulose acetate filter paper

c) chromatography paper

d) All of the above



36. what is agarose gel?


a) Cross linkage molecules

b) Purified unchanged polysaccharide

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




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Answer:-


1) B

2) C

3) B

4) B

5) D

6) A

7) D

8) D

9) C

10) B

11) C

12) D

13) B

14) A

15) A

16) C

17) C

18) A

19) A

20) C

21) D

22) A

23) A

24) C

25) D

26) C

27) B

28) C

29) B

30) C

31) D

32) B

33) B

34) D

35) D

36) D


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