Smith D C, Hider R C
Department of Chemistry, University of Essex, Wivenhoe Park, Colchester, U.K.
Biophys Chem. 1988 Aug;31(1-2):21-8. doi: 10.1016/0301-4622(88)80004-8.
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.
对分离出的蛇毒素重折叠的研究，一直是理解蛋白质折叠动力学的一项重要工具。我们在此报告了三类毒素在重折叠特性上的差异，并介绍了一种通过利用固相硫醇交换凝胶来克服二硫键错配和寡聚物形成的新方法。
