Optimizing protein folding to the native state in bacteria. |
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| Authors: | C H Schein |
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| Affiliation: | Swiss Federal Institute of Technology, Zurich. |
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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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