Disulfide-sulfhydryl interchange acceleration

The pursuit of the tertiary protein structural problem led Anfinsen to the discovery of a microsomal enzyme that catalyzes sulfhydryl-disulfide interchange and accelerates the refolding of denatured proteins which contain disulfide bonds in vitro. The kinetics of this folding accounts for the rate of folding of newly synthesized proteins in vivo. It was shown, however, that the renaturation required very dilute solutions in many cases to avoid aggregation of the protein in place of proper folding. 

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