Hi,
I've a question I'm hoping that someone will be able to answer. I have mutated the
trans-membrane domain of a protein and I've found that one relatively conservative
mutation, isoleucine->methionine, rapidly alters the mobility of the protein on
SDS-PAGE. I read somewhere that sometimes mutations can alter the interactions between
the protein and SDS, resulting in altered apparent mobilities on SDS-PAGE. If anyone
could confirm this or provide me with a reference I would be very grateful.
Thanks
Dave E-mail: CLARKE at IGMORS.U-PSUD.FR