Oxidative folding combines the formation of native disulfide bond with the conformational folding resulting in the native three-dimensional fold. Oxidative folding pathways can be described in terms of disulfide intermediate species (DIS) containing a varying number of disulfide bonds and free cysteine residues, which can also be – as opposed to the majority of protein folding states –isolated and experimentally studied. Each DIS corresponds to a family of folding states (conformations) that the given DIS can adopt in three dimensions. The oxidative folding space can be represented as a network of DIS states interconnected by disulfide interchange reactions reactions that can either create/abolish or rearrange disulfide bridges. Such networks can be used to visualize folding pathways in terms of the experimentally observed intermediates. In a number of experimentally studied cases, the observed intermediates appear as part of contiguous oxidative folding pathways.
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