Discussion
Home ‣ Biochemistry ‣ Protein Stability Comments
- Question
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
- Correct Answer
- Conformational entropy
- 1. 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
- 2. 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
- 3. 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
- 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. 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
- 6. 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
- 7. 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
- 8. 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
- 9. 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
- 10. 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
Protein Stability problems
Search Results
Correct Answer: Charged amino acids are seldom buried in the interior of a protein
Correct Answer: All of these
Correct Answer: a 10-fold increase in K decreases ?G° by about 2.3*RT
Correct Answer: rarely
Correct Answer: 5-7 other amino acids
Correct Answer: any pair of nearby atoms
Correct Answer: Hydrophobic Interactions
Correct Answer: The primary structure of ovalbumin
Correct Answer: net charge and size
Correct Answer: treated with a reducing agent and then with anionic detergent followed by fractionation by electrophoresis
Comments
There are no comments.More in Biochemistry:
Programming
Copyright ©CuriousTab. All rights reserved.