band shift in SDS PAGE with mercaptoethanol
(by muellner.markus from gmail.com)
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).
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