protein thiol groups and E.coli strains

Emir Khatipov ekhatipo at
Sun Mar 18 17:16:49 EST 2001

Could someone explain me or refer to literature or web resource about that
issue of proper folding of recombinant proteins in E.coli, and that special
strains (origami) have been developed that would allow formation of
disulfide bonds in foreign proteins and thus allow expression of functional

And what about the strains that do not allow correct folding of foreign
proteins due to non-formation of S=S? Do they exist?

I am actually interested in trying to amplifying M13 phage having gIII tail
protein with S=S on its N-terminus, both in E.coli strain that would allow
disulfide bond formation, and in the one that would not, and compare binding
of both forms of phage to my bait protein in phage displays.

Any suggestions would be highly appreciated, including any ideas on how to
break disulfide bonds.

Thank you


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