Di-sulfide bond localization

Information may not be reliable

For many proteins and peptides, disulfide bridges are prerequisite for their proper biological function. Many commercialized proteins are cross-linked by disulfide bridges that increase their resistance to destructive effects of extreme environment used in industrial processes or protect protein-based therapeutics from rapid proteolytic degradation. Manufacturing of these products must take into account oxidative refolding—a formation of native disulfide bonds by specific pairs of cysteines located throughout a sequence of linear protein.

di-sulfide bond localization plays an important role in the folding and stability of some proteins, usually proteins secreted to the extracellular medium. Since most cellular compartments are reducing environments, in general, disulfide bonds are unstable in the cytosol, with some exceptions as noted below, unless a sulfhydryl oxidase is present.