Protocol

E. coliGene Expression Protocols

Volume 205 of the series Methods in Molecular Biology™ pp 171-197

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

  • François BaneyxAffiliated withDepartment of Chemical Engineering, University of Washington
  • , Joanne L. PalumboAffiliated withDepartment of Chemical Engineering, University of Washington

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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.