Refolding of SDS-denatured proteins using amphipathic cosolvents and osmolytes

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Currently, the investigation of protein refolding processes involves several timeconsuming 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.

Original languageEnglish
Article number28.5
Pages (from-to)1 - 9
Number of pages9
JournalCurrent Protocols in Protein Science
Issue numberSUPPL.72
Publication statusPublished - 3 Sept 2013


  • Cosolvent
  • Osmolyte
  • Protein refolding
  • Sodium dodecyl sulfate

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