Unfolding and Refolding of Proteins

Abstract

In this review I first described the stability of proteins obtained from unfolding experiments and how the replacement of a specified amino acid residue with other residues in a protein affects the protein stability. Second, I described the kinetics of unfolding and refolding of proteins. The transition from folded state to unfolded state or from unfolded state to folded state is highly cooperative, and no structural intermediate is detected. Therefore, it is difficult to understand how the regular structure of the native protein is formed from the unfolded molecule. Finally I described the pathway of the disulfide bond formation from reduced proteins. © 1988, The Society of Synthetic Organic Chemistry, Japan. All rights reserved.