1. In an SDS-PAGE
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
B. proteins have the same charge-to-mass ratio
C. smaller proteins migrate more rapidly through the gel
D. all of the above
Answer: D
2. Proteins can be visualized directly in gels by
A. staining them with the dye
B. using electron microscope only
C. measuring their molecular weight
D. none of these
B. using electron microscope only
C. measuring their molecular weight
D. none of these
Answer: A
3. In SDS-PAGE, the protein sample is first
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
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
Answer: A
4. Electrophoresis of histones and myoglobin under
non-denaturing conditions (pH = 7.0) results in
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
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
Answer: C
5. In isoelectric focusing, proteins are separated on the basis
of their
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
B. relative content of negatively charged residue only
C. size
D. relative content of positively and negatively charged residue
Answer: D
GEL
ELECTROPHORESIS Questions and Answers ::
6. In a gel filtration column
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
B. large proteins elute first
C. both (a) and (b)
D. large proteins enter the beads more readily
Answer: C
7. In a native PAGE, proteins are separated on the basis of
A. net negative charge
B. net charge and size
C. net positive charges size
D. net positive charge
B. net charge and size
C. net positive charges size
D. net positive charge
Answer: B
8. The subunit molecular weight as well as the number of
subunits in the quaternary structure can be determined by
A. SDS-PAGE electrophoresis
B. gel filtration chromatography
C. combining information from (a)and (b)
D. isoelectric focusing
B. gel filtration chromatography
C. combining information from (a)and (b)
D. isoelectric focusing
Answer: C
9. Proteins are separated in an SDS-PAGE experiment on the basis
of their
A. positively charged side chains
B. molecular weight
C. negatively charged side chains
D. different isoelectric points
Answer: BB. molecular weight
C. negatively charged side chains
D. different isoelectric points
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