The solution structures of a series of conformationally restricted pentapeptides with a sequence H‐Tyr1‐Cys2‐Gly3 Phe4‐Cys5‐OH cyclic (2‐5) disulfide, where the cysteines possess either the D or L configuration, were examined by a combined approach including NMR measurements as well as MD calculations. It turned out that at least one low energy conformer of H‐Tyr1‐Cys2‐Gly3‐Phe4‐Cys5‐OH cyclic (2‐5) disulfide (DCDCE), as well as one conformer out of the group of calculated conformers for H‐Tyr1‐D‐Cys2‐Gly3‐Phe4‐Cys5‐OH cyclic (2‐5) disulfide (DCLCE), satisfies the NMR data obtained in this study, whereas for the derivative H‐Tyrl‐Cys2‐Gly3‐Phe4‐Cys5‐OH cyclic (2‐5) disulfide, which contains solely L‐Cys (LCLCE), there is no single structure compatible with the NMR data. © Munksgaard 1996.