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- Question
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
- Correct Answer
- histones migrate to the cathode and myoglobin migrates to the anode
- 1. 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
- 2. 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
- 3. 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
- 4. 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
- 5. 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
- 6. 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
- 7. 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
- 8. 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
- 9. 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
- 10. 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
Gel Electrophoresis problems
Search Results
Correct Answer: treated with a reducing agent and then with anionic detergent followed by fractionation by electrophoresis
Correct Answer: net charge and size
Correct Answer: The primary structure of ovalbumin
Correct Answer: Hydrophobic Interactions
Correct Answer: any pair of nearby atoms
Correct Answer: molecular weight
Correct Answer: all of the above
Correct Answer: combining information from (a)and (b)
Correct Answer: relative content of positively and negatively charged residue
Correct Answer: both (a) and (b)
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