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- September 23, 2016 at 3:50 am
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 analysis.
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