Unit

UNIT 28.5 Refolding of SDS-Denatured Proteins Using Amphipathic Cosolvents and Osmolytes

  1. Guillaume Roussel,
  2. Emmanuel Tinti,
  3. Eric Perpète,
  4. Catherine Michaux

Published Online: 1 APR 2013

DOI: 10.1002/0471140864.ps2805s72

Current Protocols in Protein Science

Current Protocols in Protein Science

How to Cite

Roussel, G., Tinti, E., Perpète, E. and Michaux, C. 2013. Refolding of SDS-Denatured Proteins Using Amphipathic Cosolvents and Osmolytes. Current Protocols in Protein Science. 72:28.5:28.5.1–28.5.9.

Author Information

  1. Department of Chemistry, Unité de Chimie Physique Théorique et Structurale, University of Namur, Namur, Belgium

Publication History

  1. Published Online: 1 APR 2013
  2. Published Print: APR 2013

Abstract

Currently, the investigation of protein refolding processes involves several time-consuming stages that require large amounts of protein and costly chemicals. Consequently, there is great interest in developing new approaches to the study of protein renaturation that are more technically and economically feasible. It has recently been reported that certain cosolvents are able to modulate the denaturing properties of sodium dodecyl sulfate (SDS) and induce the refolding of proteins. This unit presents a protocol to study and follow the renaturation of a protein (membrane or soluble) starting from a native or SDS-unfolded state using a variety of candidate cosolvents and osmolytes. Curr. Protoc. Protein Sci. 72:28.5.1-28.5.9. © 2013 by John Wiley & Sons, Inc.

Keywords:

  • sodium dodecyl sulfate;
  • cosolvent;
  • osmolyte;
  • protein refolding