If SDS denaturates proteins, how can they still be detected in a western blot?

Question

If SDS denaturates proteins, how can they still be detected in a western blot?

In: Biology

Answer 1

Denaturing decharges and unfolds protiens (mostly) it doesn’t break them into pieces.

The gel electrophoresis section separates out protiens by size (because the remaining charge is evenly distributed accross the protein), not conformation.

If you didn’t denature the intrinsic charge of the folded protien would interfere.