UNIT 28.5 Refolding of SDS-Denatured Proteins Using Amphipathic Cosolvents and Osmolytes
Published Online: 1 APR 2013
Copyright © 2013 by John Wiley & Sons, Inc.
Lab Protocol Title
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.
- Published Online: 1 APR 2013
- Published Print: APR 2013
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.
- sodium dodecyl sulfate;
- protein refolding