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The conformations of native proteins are in principle, and in most cases, dictated by the law of thermodynamics. Accordingly, a native protein must always exist in equilibrium with a minor concentration of nonnative (denatured) conformational isomers even at nondenaturing conditions. The presence of an infinitesimal quantity of nonnative conformational isomers at physiological conditions is biologically...
Oxidative folding of fully reduced hirudin (R-Hir, six cysteines) undergoes two distinct stages. A first stage of nonspecific disulfide formation promoted by oxidase converts R-Hir to form 3-disulfide scrambled hirudins (X-Hir) as obligatory intermediates. A second stage of disulfide shuffling catalyzed by isomerase converts X-Hir to the native hirudin (N-Hir). The model of hirudin folding is utilized...
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