Hi
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.
Thanks
James.
