The goal of this review has been to present different chemical approaches for the formation
of disulfide bonds in synthetic peptides and small proteins. Three general types of …

abstract Disulfide bridges play a crucial role in the folding and structural stabilization of
many important extracellular peptide and protein molecules, including hormones, enzymes …

The formation of disulfide bridges is often a crucial final stage in peptide synthesis. There is
compelling evidence that the disulfide pattern can be critical in the folding and structural …

The controlled formation of intramolecular disulfide bridges in peptides, while avoiding
unwanted oligomerization, is a significant challenge. Ellman's reagent, 5, 5 '-dithiobis (2 …

A selective and efficient method for disulfide bond formation in peptides by dimethyl
sulfoxide (DMSO) is described. Facile disulfide bond formation by DMSO in aqueous …

Publisher Summary This chapter discusses the three types of the available thiol modification
reagents that produce protein mixed disulfides: disulfides, alkyl thiol sulfonates, and …

Disulfide bonds play an important role in both proteins and peptides. They cause
conformational constraints and increase the stability of such molecules. In nature, disulfide …

Abstract Bis (2-mercaptoethyl) sulfone (BMS) and N, N′-dimethyl-N, N′-bis
(mercaptoacetyl) hydrazine (DMH) reduce native disulfide bonds in proteins at pH 7 …

The disulfide bond plays an important role in biological systems. It defines global
conformation, and ultimately the biological activity and stability of the peptide or protein. It is …

Publisher Summary Protein disulfide formation in vivo as a post-translational modification is
expected to depend upon both the conformation and the environment of the polypeptide …