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Improving Heterologous Protein Folding via Molecular Chaperone and Foldase Co-Expression

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E. coliGene Expression Protocols

Part of the book series: Methods in Molecular Biology™ ((MIMB,volume 205))

Abstract

Protein folding in the viscous and crowded environment of the cell is very different from in vitro processes in which a single protein is allowed to refold at low concentration in an optimized buffer. Although Anfinsen's observation that all the information necessary for a protein to reach a proper conformation is contained in the amino acid sequence (1) remains unchallenged, it has recently become obvious that the efficient in vivo folding of subsets of cellular proteins, as well as that of most recombinant proteins, requires the assistance of folding modulators that can be broadly classified as molecular chaperones and foldases.

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  1. Department of Chemical Engineering, University of Washington, Seattle, WA

    François Baneyx & Joanne L. Palumbo

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  1. François Baneyx
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  1. Applied Molecular Evolution, San Diego, CA, USA

    Peter E. Vaillancourt

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Baneyx, F., Palumbo, J.L. (2003). Improving Heterologous Protein Folding via Molecular Chaperone and Foldase Co-Expression. In: Vaillancourt, P.E. (eds) E. coliGene Expression Protocols. Methods in Molecular Biology™, vol 205. Humana Press. https://doi.org/10.1385/1-59259-301-1:171

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  • DOI: https://doi.org/10.1385/1-59259-301-1:171

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