joerg.freigang at uni-konstanz.de
Thu Nov 7 10:26:17 EST 1996
I am trying to refold a protein belonging to the IGSF from inclusion
bodies. The protein contains two disulfide bonds and a his-tag. I tried
the refolding procedure developed by R. Rudolph for Fab-fragments as
well as some other standart refolding procedures, but I couldn't get any
detectable amounts of monodispers protein.
Any suggestions what the problem could be and what else should be tried?
Even 1 % of correctly folded protein would be enough.
email: Joerg.Freigang at uni-konstanz.de Tel: +49 7531 88 2211
Fakultaet fuer Biologie, Universitaet Konstanz
Postfach 5560, M 656, D-78434 Konstanz, Germany
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