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Updated: May 12, 2026

Method for Efficient Refolding and Purification of Chemoreceptor Ligand Binding Domain
Published on: December 12, 2017
Refolding of SDS-denatured proteins using amphipathic cosolvents and osmolytes
Guillaume Roussel1, Emmanuel Tinti, Eric Perpète
1Department of Chemistry, Unité de Chimie Physique Théorique et Structurale, University of Namur, Namur, Belgium.
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.
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