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Protein Stability problems


  • 1. For the unfolding reaction of Protein G, ∆H° =210.6 kJ/mol, this means that

  • Options
  • A. unfolding is favored enthalpically
  • B. folding is favored enthalpically
  • C. the entropy is positive at all temperatures
  • D. the entropy is negative at all temperatures
  • Discuss
  • 2. The correlation between free energy ?G transfer between the aqueous/organic phases and the surface area of amino acid residues

  • Options
  • A. reflects the reduction in solvent-accessible area during protein folding
  • B. is only meaningful for the polar amino acids
  • C. ignores the important contribution of the peptide bond
  • D. is similar to effects seen with SDS denaturation
  • Discuss
  • 3. Buried hydrophobic side chains in a globular protein fit into a hole formed by the side chains of

  • Options
  • A. 1-3 other amino acids
  • B. 5-7 other amino acids
  • C. 9-12 other amino acids
  • D. 13-15 other amino acids
  • Discuss
  • 4. Unpaired H-bond donors and acceptors are found in the hydrophobic core of a protein

  • Options
  • A. only at the ends of a-helices
  • B. only at the turns connecting p-strands
  • C. only on Pro residues
  • D. rarely
  • 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. 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
  • 7. 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
  • 8. 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
  • 9. 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
  • 10. 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

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