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Home Biochemistry Protein Stability Comments

  • Question
  • 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

  • Correct Answer
  • Hydrophobic Interactions 


  • Protein Stability problems


    Search Results


    • 1. Attractive Vander Waals forces occur between

    • Options
    • A. apolar molecules in the liquid state
    • B. any pair of nearby atoms
    • C. polar molecules in the solid state
    • D. only if other forces are less favorable
    • Discuss
    • 2. Which of the following forces is the most unfavorable for protein folding?

    • Options
    • A. Conformational entropy
    • B. Hydrophobic interactions
    • C. Vander Waals interactions
    • D. Electrostatic interactions
    • Discuss
    • 3. Which of the following is the most correct?

    • Options
    • A. Charged amino acids are never buried in the interior of a protein
    • B. Charged amino acids are seldom buried in the interior of a protein
    • C. All hydrophobic amino acids are buried when a protein folds
    • D. Tyrosine is only found in the interior of proteins
    • Discuss
    • 4. At the midpoint of a temperature transition curve,

    • Options
    • A. half of the protein is denatured
    • B. Keq = 1.0 and ?G = 0
    • C. [Native] = [Unfolded]
    • D. All of these
    • Discuss
    • 5. Since ?G° = -RTlnK

    • Options
    • A. a 10-fold increase in K decreases ?G° by about 10-fold
    • B. a 10-fold decrease in K decreases ?G° by about 2.3*RT
    • C. a 10-fold increase in K decreases ?G° by about 2.3*RT
    • D. a 10-fold decrease in K increases ?G° by about 10-fold
    • Discuss
    • 6. 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
    • 7. 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
    • 8. 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
    • 9. 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
    • 10. 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
    • Discuss


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