Refolding of SDS-denatured proteins using amphipathic cosolvents and osmolytes.

Guillaume Roussel, Emmanuel Tinti, Eric Perpète, Catherine Michaux

Index: Curr. Protoc. Protein Sci. Chapter 28 , Unit28.5, (2013)

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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.