Thiol exchange catalysed refolding of small proteins utilizing solid-phase supports.
The study of isolated snake toxin refolding has been a valuable tool in the understanding of protein folding dynamics. We report here differences in the refolding characteristics of three toxin classes and introduce a novel method for overcoming disulphide mismatching and oligomer formation by utilizing solid-phase thiol exchange gels.
Smith
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Department of Chemistry, University of Essex, Wivenhoe Park, Colchester, U.K.
Hider
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D002851:Chromatography, High Pressure Liquid; D002942:Circular Dichroism; D004546:Elapid Venoms; D004591:Electrophoresis, Polyacrylamide Gel; D007525:Isoelectric Focusing; D007700:Kinetics; D011487:Protein Conformation; D013438:Sulfhydryl Compounds
D004546:Elapid Venoms; D013438:Sulfhydryl Compounds