Pick all that are TRUE regarding analysis of quaternary structures of proteins using polyacrylamide electrophoresis: I. The added β-mercaptoethanol disrupts S--S bonds bridging the polypeptide chains causing the appearance of higher Rf bands compared to the native protein run. II. Heating up any protein before subjecting to SDS-PAGE will always result in the formation of more than one band. III. A good asymmetrical gel layout would be : (Lane 1) MW ladder, (2) native protein, (3) protein + β-ME, (4) protein + HCL, (5) protein + β-ME + HCl. IV. Formation of a single band in the protein + β-ME + HCl run, whose Rf is lower than the native run, could be indicative that the protein is a homodimer.
Pick all that are TRUE regarding analysis of quaternary structures of proteins
using polyacrylamide electrophoresis:
I. The added β-mercaptoethanol disrupts S--S bonds bridging the
polypeptide chains causing the appearance of higher Rf bands
compared to the native protein run.
II. Heating up any protein before subjecting to SDS-PAGE will always
result in the formation of more than one band.
III. A good asymmetrical gel layout would be : (Lane 1) MW ladder, (2)
native protein, (3) protein + β-ME, (4) protein + HCL, (5) protein +
β-ME + HCl.
IV. Formation of a single band in the protein + β-ME + HCl run, whose
Rf is lower than the native run, could be indicative that the protein is
a homodimer.
A. I only
B. I and II
C. II and IIV
D. None is true.
pls explain
Step by step
Solved in 2 steps with 2 images
