Jenny have a look at our REFOLD database: http://refold.med.monash.edu.au you can find several refolding protocols in there for immunoglobulin folds (you can blast your sequence against the refold database) cheers ashley
-- Ashley Buckle Ph.D NHMRC Senior Research Fellow The Department of Biochemistry and Molecular Biology School of Biomedical Sciences, Faculty of Medicine & Victorian Bioinformatics Consortium (VBC) Monash University, Clayton, Vic 3800 Australia http://www.med.monash.edu.au/biochem/staff/abuckle.html iChat/AIM: blindcaptaincat skype: ashley.buckle Tel: (613) 9902 0269 (office) Tel: (613) 9905 1653 (lab) Fax : (613) 9905 4699 ----- Original Message ----- From: Jenny <[EMAIL PROTECTED]> Date: Thursday, July 10, 2008 11:00 am Subject: [ccp4bb] how to promote folding for an unfolded protein To: CCP4BB@JISCMAIL.AC.UK > Dear CCP4 community, > > Sorry for this off-topic protein purification problem.I'm trying to > purifyan immunoglobulin-like beta sheet protein with a c-terminus > HIS construct. > The protein expressed both in the supernat and pellet ( majority ). I > purified the supernat and after run gel filtration, it's in the > void volume. > I also tried to purify from the pellet,and do dialysis refolding ( > with and > without L-arg ), after overnight dialysis, I run the gel filtration > column,the apparent molecular weight looks like dimer/trimer. But > when I did a CD > scan of the protein, it's showing an unfolded protein profile.I was > wondering if there is anyway to promote folding,or if anyway that > can make > some mutations to make it foldable.Any input would be useful. > > Thanks a lot. > > Jenny >
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