Disulfide bond formation as a probe for folding mechanism and non-native conformational state of proteins

Abstract

Disulfide bond formation has been used as a useful probe for analyzing protein folding mechanisms, because disulfide intermediates can be trapped in stable forms. In addition, the analysis for the distribution of disulfide isomers that are formed by intrachain sufhydryl/disulfide exchange reactions provides crucial information about non-native conformational states of globular proteins. Recent results from these analyses are reviewed