In vitro protein refolding by chromatographic procedures

Protein Expr Purif. 2004 Jan;33(1):1-10. doi: 10.1016/j.pep.2003.08.023.

Abstract

In vitro protein refolding is still a bottleneck in both structural biology and in the development of new biopharmaceuticals, especially for commercially important polypeptides that are overexpressed in Escherichia coli. This review focuses on protein refolding methods based on column procedures because recent advances in chromatographic refolding have shown promising results.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Chaperonins / chemistry
  • Chromatography, Gel / methods*
  • Escherichia coli / metabolism
  • Humans
  • Inclusion Bodies / metabolism
  • Liposomes / chemistry
  • Polyethylene Glycols / chemistry
  • Protein Folding*
  • Protein Renaturation*
  • Urea / chemistry

Substances

  • Liposomes
  • Polyethylene Glycols
  • Urea
  • Chaperonins