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Refolding SDS-denatured proteins by the addition of amphipathic cosolvents.

Journal of molecular biology (2007-12-18)
Catherine Michaux, Neil C Pomroy, Gilbert G Privé
ABSTRACT

Sodium dodecyl sulfate (SDS) is a highly effective and widely used protein denaturant. We show that certain amphipathic cosolvents such as 2-methyl-2,4-pentanediol (MPD) can protect proteins from SDS denaturation, and in several cases can refold proteins from the SDS-denatured state. This cosolvent effect is observed with integral membrane proteins and soluble proteins from either the alpha-helical or the beta-sheet structural classes. The SDS/MPD system can be used to study processes involving native protein states, and we demonstrate the reversible thermal denaturation of the outer membrane protein PagP in an SDS/MPD buffer. MPD and related cosolvents can modulate the denaturing properties of SDS, and we describe a simple and effective method to recover refolded, active protein from the SDS-denatured state.

MATERIALS
Product Number
Brand
Product Description

Sigma-Aldrich
Hexylene glycol, 99%
Sigma-Aldrich
Hexylene glycol, puriss., ≥99.0% (GC)
Sigma-Aldrich
Hexylene glycol, BioXtra, ≥99% (GC)

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