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Replacement of disulfide bridges with diselenide bridges is increasingly common to improve the stability, foldability, and structural refinement of the cysteine-rich polypeptides. Even though the global structural features are similar due to the replacement of disulfide with diselenide, the local conformational differences have been reported in a few polypeptides. The current report has used the constrained vicinal cysteine disulfide as the model to access the influence of the replacement of disulfides with diselenide on the local conformations. Using the density functional theory (DFT), structures of dipeptide vicinal loops are optimized by systematically replacing sulfur with selenium. Conformations of the disulfide/selenosulfide/diselenide were identified using the side-chain torsional angle χ |
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