How are Proteins Denatured in SDS-PAGE

Question

How are proteins denatured in SDS-PAGE?
A)detergent and high temperature
B)high temperature only
C)acylamide
D)electrical charge

Accepted Answer

SDS-PAGE involves denaturing proteins with the use of a detergent (SDS) and high temperature. This causes the proteins to unfold and become negatively charged, allowing them to separate based on size when an electrical current is applied during gel electrophoresis. Acrylamide is used to create the gel matrix and does not denature the proteins on its own. Electrical charge is used to separate the denatured and negatively charged proteins based on size, but it is not the cause of denaturation.