The intrinsic conformational preferences of proline analogues having double bonds between carbon atoms in their rings have been investigated using quantum mechanical calculations at the B3LYP/6-31+G(d,p) level. For this purpose, the potential energy surface of the N-acety-N′-methylamide derivatives of three dehydroprolines (proline analogues unsaturated at α,β; β,γ; and γ,δ) and pyrrole (proline analogue with unsaturations at both α,β and γ,δ) have been explored, and the results are compared with those obtained for the derivative of the nonmodified proline. We found that the double bonds affect the ring puckering and the geometric internal parameters, even though the backbone conformation was influenced the most. Results indicate that the formation of double bonds between carbon atoms in the pyrrolidine ring should be considered as an effective procedure to restrict the conformational flexibility of prolines. Interestingly, we also found that the N-acetyl-N′-methylamide derivative of pyrrole shows a high probability of having a cis peptide bond preceding the proline analogue.