Hello Amberites,
I have a quick question regarding oligeric interactions in proteins. I know that if we model a protein in 8M urea, that the protein should unfold. But if I have a dimer, there should be something less harsh that will let the two monomers separate. I thought I might have known this from undergrad some years ago, but don't have a quick fix handy. Perhaps a mild combination of salt and/or pH? If any of you have some ideas, I'd be all ears.
Main reason for asking is, I have an xtal structure that is a dimer, but I want to run some kinetic analyses on the monomer, and rather than just stripping the dimer in half, I thought that I could set up the assay conditions to represent those that would support a the monomer. Not eloquently worded, but if anyone has any ideas, please advise.
Sean
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Received on Sun Mar 04 2007 - 06:08:12 PST
