Review
doi: 10.1016/0958-1669(91)90046-8.
Optimizing protein folding to the native state in bacteria
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- PMID: 1367729
- DOI: 10.1016/0958-1669(91)90046-8
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Review
Optimizing protein folding to the native state in bacteria
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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