Gel Electrophoresis(Biochemistry ) Questions and Answers

Question 1. Electrophoresis of histones and myoglobin under non-denaturing conditions (pH = 7.0) results in
  1.    both proteins migrate to the cathode
  2.    histones migrate to the cathode and myoglobin migrates to the anode
  3.    both proteins migrate to the anode
  4.    histones migrate to the anode and myoglobin migrates to the cathode
Explanation:-
Answer: Option B. -> histones migrate to the cathode and myoglobin migrates to the anode
Question 2. Proteins can be visualized directly in gels by
  1.    using electron microscope only
  2.    measuring their molecular weight
  3.    staining them with the dye
  4.    none of these
Explanation:-
Answer: Option C. -> staining them with the dye
Question 3. In an SDS-PAGE
  1.    proteins have the same charge-to-mass ratio
  2.    smaller proteins migrate more rapidly through the gel
  3.    All of these
  4.    proteins are denatured by the SDS
Explanation:-
Answer: Option C. -> All of these
Question 4. In isoelectric focusing, proteins are separated on the basis of their
  1.    relative content of positively and negatively charged residue
  2.    size
  3.    relative content of negatively charged residue only
  4.    relative content of positively charged residue only
Explanation:-
Answer: Option A. -> relative content of positively and negatively charged residue
Question 5. In SDS-PAGE, the protein sample is first
  1.    treated with a oxidizing agent and then with anionic detergent followed by fractionation by electrophoresis
  2.    fractionated by electrophoresis then treated with an oxidizing agent followed by anionic detergent.
  3.    None of these
  4.    treated with a reducing agent and then with anionic detergent followed by fractionation by electrophoresis
Explanation:-
Answer: Option D. -> treated with a reducing agent and then with anionic detergent followed by fractionation by electrophoresis
Question 6. In a gel filtration column
  1.    large proteins enter the beads more readily
  2.    smaller proteins enter the beads more readily
  3.    large proteins elute first
  4.    both (a) and (b)
Explanation:-
Answer: Option D. -> both (a) and (b)
Question 7. Proteins are separated in an SDS-PAGE experiment on the basis of their
  1.    positively charged side chains
  2.    negatively charged side chains
  3.    molecular weight
  4.    different isoelectric points
Explanation:-
Answer: Option C. -> molecular weight
Question 8. In a native PAGE, proteins are separated on the basis of
  1.    net positive charge
  2.    net negative charge
  3.    net positive charges size
  4.    net charge and size
Explanation:-
Answer: Option D. -> net charge and size
Question 9. The subunit molecular weight as well as the number of subunits in the quaternary structure can be determined by
  1.    isoelectric focusing
  2.    SDS-PAGE electrophoresis
  3.    combining information from (a)and (b)
  4.    gel filtration chromatography
Explanation:-
Answer: Option C. -> combining information from (a)and (b)
Question 10.  In an SDS-PAGE
  1.    proteins are denatured by the SDS
  2.    proteins have the same charge-to-mass ratio
  3.    smaller proteins migrate more rapidly through the gel
  4.    all of the above
Explanation:-
Answer: Option D. -> all of the above
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