band shift in SDS PAGE with mercaptoethanol

MarkusM via (by muellner.markus from
Wed Aug 8 03:48:38 EST 2007

Note that it is the radius, not the MW, that determines the position of a
protein in a  
> SDS-PAGE gel.

Thanks! I guess this is the reason I was surprised...
My reasoning was that an unfolded protein would be able to bind more SDS and
therefore receive more of a negative charge than a folded protein (hence the
folded protein should stay behind its unfolded version on a gel).

View this message in context:
Sent from the - Methods mailing list archive at

More information about the Methods mailing list