title: Thiol exchange catalysed refolding of small proteins utilizing solid-phase supports.
abstract: 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.
authors.affiliation: Department of Chemistry, University of Essex, Wivenhoe Park, Colchester, U.K.
authors.forename: D C
authors.initials: DC
authors.lastname: Smith
authors.forename: R C
authors.initials: RC
authors.lastname: Hider
mesh_terms: 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
chemical_list: D004546:Elapid Venoms; D013438:Sulfhydryl Compounds