Optimizing protein folding to the native state in bacteria

Catherine H. Schein

doi:10.1016/0958-1669(91)90046-8

Optimizing protein folding to the native state in bacteria

Catherine H. Schein

Research output: Contribution to journal › Article › peer-review

51 Scopus citations

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.

Original language	English (US)
Pages (from-to)	746-750
Number of pages	5
Journal	Current Opinion in Biotechnology
Volume	2
Issue number	5
DOIs	https://doi.org/10.1016/0958-1669(91)90046-8
State	Published - Oct 1991
Externally published	Yes

ASJC Scopus subject areas

Biotechnology
Bioengineering
Biomedical Engineering

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10.1016/0958-1669(91)90046-8

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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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Optimizing protein folding to the native state in bacteria

Abstract

ASJC Scopus subject areas

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