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Review
. 1991 Oct;2(5):746-50.
doi: 10.1016/0958-1669(91)90046-8.

Optimizing protein folding to the native state in bacteria

C H Schein  1
Affiliations
Review

Optimizing protein folding to the native state in bacteria

C H Schein. Curr Opin Biotechnol. 1991 Oct.

Abstract

A correctly folded protein is usually both active and soluble. This review focuses on novel ways to improve the folding of recombinant proteins during production in bacteria and includes a few tips for refolding proteins. Major results in correlating protein primary structure with proper folding and stability, and the production of viral antigens and antibodies in bacteria are also discussed.

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