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Home Biochemistry Gel Electrophoresis Comments

  • Question
  • Proteins are separated in an SDS-PAGE experiment on the basis of their


  • Options
  • A. positively charged side chains
  • B. molecular weight
  • C. negatively charged side chains
  • D. different isoelectric points

  • Correct Answer
  • molecular weight 


  • Gel Electrophoresis problems


    Search Results


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

    • Options
    • 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
    • Discuss
    • 2. In SDS-PAGE, the protein sample is first

    • Options
    • 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
    • Discuss
    • 3. In a native PAGE, proteins are separated on the basis of

    • Options
    • A. net negative charge
    • B. net charge and size
    • C. net positive charges size
    • D. net positive charge
    • Discuss
    • 4. If the egg white protein, ovalbumin, is denatured in a hard-boiled egg, then which of the following is least affected?

    • Options
    • A. The primary structure of ovalbumin
    • B. The secondary structure of ovalbumin
    • C. The tertiary structure of ovalbumin
    • D. The quaternary structure of ovalbumin
    • Discuss
    • 5. Which of the following forces is the most favorable for protein folding?

    • Options
    • A. Conformational entropy
    • B. Hydrophobic Interactions
    • C. Vander Waals interactions
    • D. Hydrogen bonds
    • Discuss
    • 6. In an SDS-PAGE

    • Options
    • 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
    • Discuss
    • 7. The subunit molecular weight as well as the number of subunits in the quaternary structure can be determined by

    • Options
    • A. SDS-PAGE electrophoresis
    • B. gel filtration chromatography
    • C. combining information from (a)and (b)
    • D. isoelectric focusing
    • Discuss
    • 8. In isoelectric focusing, proteins are separated on the basis of their

    • Options
    • 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
    • Discuss
    • 9. In a gel filtration column

    • Options
    • A. smaller proteins enter the beads more readily
    • B. large proteins elute first
    • C. both (a) and (b)
    • D. large proteins enter the beads more readily
    • Discuss
    • 10. Proteins can be visualized directly in gels by

    • Options
    • A. staining them with the dye
    • B. using electron microscope only
    • C. measuring their molecular weight
    • D. none of these
    • Discuss


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