“Influence of ionisation on the conformational preferences of peptide models. Ramachandran surfaces of N-formyl-glycine amide and N-formyl-alanine amide radical cations

Gil, A.; Sodupe, M.*; Bertran, J.* J. Comput. Chem. 2009, 30(12), 1771.

Ramachandran maps of neutral and ionized HCO–Gly–NH2 and HCO–Ala–NH2 peptide models have been built at the B3LYP/6-31++G(d,p) level of calculation. Direct optimizations using B3LYP and the recently developed MPWB1K functional have also been carried out, as well as single-point calculations at the CCSD(T) level of theory with the 6-311++G(2df,2p) basis set. Results indicate that for both peptide models ionization can cause drastic changes in the shape of the PES in such a way that highly disallowed regions in neutral PES become low-energy regions in the radical cation surface. The structures localized in such regions, equation image and equation image are highly stabilized due to the formation of 2-centre-3-electron interactions between the two carbonyl oxygens. Inclusion of solvent effects by the conductor-like polarizable continuum model (CPCM) shows that the solute-solvent interaction energy plays an important role in determining the stability order.

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