Why are proteins separated on an SDS polyacrylamide gel equally attracted to the positive electrode?
A)They carry a relatively uniform positive charge distribution
B)They carry a relatively uniform negative charge distribution.
C)They are all the same molecular weight.
D)They are all the same size.
E)They all have the same degree of hydrophobicity.

Question

Quizplus · Accepted Answer

SDS is a negatively charged detergent that binds to and denatures proteins, causing them to unfold and become negatively charged. This results in proteins having a relatively uniform negative charge distribution, which causes them to be equally attracted to the positively charged electrode during electrophoresis.

Why Are Proteins Separated on an SDS Polyacrylamide Gel Equally