Protein purification using guanidinum hydrochloride

James jsg at
Wed Jan 21 08:55:10 EST 1998


I've purified a recombinant protein from inclusion bodies formed in BL21
E. coli, and solubilised it in 6 M GuHCl. I now need to refold the
protein; does anyone have any tips on temperature, rate of GuHCl dilution,
etc., to optimise the formation of soluble refolded monomer? My protein in
naturally monomeric, and I'd like it to stay that way!

And advice gratefully received.



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