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MCQs

Total Questions : 20 | Page 2 of 2 pages
Question 11.  
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 migrates to the cathode
  3.    histones migrate to the cathode and myoglobin migrates to the anode
  4.    both proteins migrate to the cathode
 Discuss Question
Answer: Option C. -> histones migrate to the cathode and myoglobin migrates to the anode
Question 12.  In isoelectric focusing, proteins are separated on the basis of their
  1.    relative content of positively charged residue only
  2.    relative content of negatively charged residue only
  3.    size
  4.    relative content of positively and negatively charged residue
 Discuss Question
Answer: Option D. -> relative content of positively and negatively charged residue
Question 13.  Proteins 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
 Discuss Question
Answer: Option A. -> staining them with the dye
Question 14.  In SDS-PAGE, the protein sample is first
  1.    treated with a reducing 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.    treated with a oxidizing agent and then with anionic detergent followed by fractionation by electrophoresis
  4.    none of the above
 Discuss Question
Answer: Option A. -> treated with a reducing agent and then with anionic detergent followed by fractionation by electrophoresis
Question 15.  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
 Discuss Question
Answer: Option C. -> both (a) and (b)
Question 16.  In a native PAGE, proteins are separated on the basis of
  1.    net negative charge
  2.    net charge and size
  3.    net positive charges size
  4.    net positive charge
 Discuss Question
Answer: Option B. -> net charge and size
Question 17.  The subunit 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
 Discuss Question
Answer: Option C. -> combining information from (a)and (b)
Question 18.  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 points
 Discuss Question
Answer: Option B. -> molecular weight
Question 19. . The subunit 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
 Discuss Question
Answer: Option C. -> combining information from (a)and (b)
Question 20. . 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 points
 Discuss Question
Answer: Option B. -> molecular weight

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