Solvent effects on the conformational behavior of model peptides. A comparison between different continuum models

Solvent effects on the conformational behavior of the simplest analogue of glycine in a peptide have been investigated by a hybrid Hartree-Fock density functional approach, coupled to latest generation continuum models. The results obtained for the isolated molecule compare favorably with the most sophisticated post-Hartree-Fock approaches. The effect of solvation is to flatten out the gas phase surface, reducing the gap between hydrogen-bonded and helical structures. Comparable trends are obtained by two different continuum models employing realistic shapes of the cavity made in the solvent.