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Chaperonin assisted polypeptide folding and assembly: implications for the production of functional proteins in
A A Gatenby1, P V Viitanen, G H Lorimer
1Central Research & Development Department, E. I. Du Pont de Nemours & Co., Experimental Station, Wilmington, DE 19880-0402.
Trends in Biotechnology
|December 1, 1990
Abstract:
Production of biologically active foreign proteins with correct three-dimensional structures is often difficult in bacteria. Recent advances demonstrate that, for some proteins at least, their correct folding and assembly is facilitated by a class of proteins known as molecular chaperones. An understanding of the function of molecular chaperones may assist in the synthesis in bacteria of functional foreign proteins produced by recombinant techniques.