Diversity of folding pathways and folding models of disulfide proteins.

Comprehensive understanding of the mechanism of protein folding requires the elucidation of both a folding pathway and a folding model. This entails characterization of the properties and structures of folding intermediates populated along the folding pathway, as well as the formation and interplay of secondary structures and tertiary structures along the course of folding. Using the conventional unfolding-refolding technique, there are limitations of acquiring these data in detail because of the inherent difficulty of trapping and analysis of folding intermediates. The technique of oxidative folding, in contrast, permits trapping, isolation, and further structural characterization of folding intermediates at any stage of the folding process. In this brief review, we present the potential of the technique of oxidative folding for concurrent analysis of both folding pathways and folding models.