Refolding of SDS-denatured proteins using amphipathic cosolvents and osmolytes

Research output: Contribution to journalArticle

Abstract

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
Volume28.5
Issue numberSUPPL.72
DOIs
Publication statusPublished - 3 Sep 2013

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Protein Renaturation
Protein Refolding
Sodium Dodecyl Sulfate
Membrane Proteins
Proteins

Keywords

  • Cosolvent
  • Osmolyte
  • Protein refolding
  • Sodium dodecyl sulfate

Cite this

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Refolding of SDS-denatured proteins using amphipathic cosolvents and osmolytes. / Roussel, Guillaume; Tinti, Emmanuel; Perpète, Eric; Michaux, Catherine.

In: Current Protocols in Protein Science, Vol. 28.5, No. SUPPL.72, 28.5, 03.09.2013, p. 1 - 9.

Research output: Contribution to journalArticle

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