PMID:18083190
| Citation |
Michaux, C, Pomroy, NC and Privé, GG (2008) Refolding SDS-denatured proteins by the addition of amphipathic cosolvents. J. Mol. Biol. 375:1477-88 |
|---|---|
| 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. |
| Links |
PubMed Online version:10.1016/j.jmb.2007.11.026 |
| Keywords |
Acyltransferases/metabolism; Animals; Bacterial Outer Membrane Proteins/isolation & purification; Bacterial Outer Membrane Proteins/metabolism; Bacteriorhodopsins/chemistry; Buffers; Carbonic Anhydrase II/chemistry; Chickens; Dose-Response Relationship, Drug; Escherichia coli Proteins/metabolism; Glycols/chemistry; Halobacterium salinarum/chemistry; Hot Temperature; Humans; Hydrophobic and Hydrophilic Interactions; Inclusion Bodies/chemistry; Muramidase/chemistry; Protein Conformation/drug effects; Protein Denaturation; Protein Folding; Protein Renaturation; Protein Structure, Secondary; Sodium Dodecyl Sulfate/pharmacology; Solubility; Solvents/chemistry; Surface-Active Agents/pharmacology |
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