A new scheme for determining the intramolecular seven-membered ring N-H•••O=C hydrogen-bonding energies of glycine and alanine peptides -: art. no. 024307

In this paper a new scheme was proposed to calculate the intramolecular hydrogen-bonding energies in peptides and was applied to calculate the intramolecular seven-membered ring N-H center dot O = C hydrogen-bonding energies of the glycine and alanine peptides. The density-functional theory B3LYP/6-31G(d) and B3LYP/6-311G(d,p) methods and the second-order Moller-Plesset perturbation theory MP2/6-31G(d) method were used to calculate the optimal geometries and frequencies of glycine and alanine peptides and related structures. MP2/6-311++G(d,p), MP2/6-311++G(3df,2p), and MP2/aug-cc-pVTZ methods were then used to evaluate the single-point energies. It was found that the B3LYP/6-31G(d), MP2/6-31G(d), and B3LYP/6-311G(d,p) methods yield almost similar structural parameters for the conformers of the glycine and alanine dipeptides. MP2/aug-cc-pVTZ predicts that the intramolecular seven-membered ring N-H center dot O = C hydrogen-bonding strength has a value of 5.54 kcal/mol in glycine dipeptide and 5.73 and 5.19 kcal/mol in alanine dipeptides, while the steric repulsive interactions of the seven-membered ring conformers are 4.13 kcal/mol in glycine dipeptide and 6.62 and 3.71 kcal/mol in alanine dipeptides. It was also found that MP2/6-311++G(3df,2p) gives as accurate intramolecular N-H center dot O = C hydrogen-bonding energies and steric repulsive interactions as the much more costly MP2/aug-cc-pVTZ does. (c) 2005 American Institute of Physics.