Hydrogen bonds: a comparison of semiempirical and ab initio treatments

H-bonding interactions calculated using the AM1, PM3 and SAM1 semiempirical molecular orbital methods are compared with the best available ab initio calculations for several intermolecular interactions of interest: acetic acid dimers, water/ acetylene, water/HCN, formaldehyde/acetylene, formaldehyde/HCN, ozone/acetylene, ozone/HCN, acetylacetone, melamine/ cyanuric acid, and nitromethane/ammonia. Experimental values are also presented where available. The energetic comparisons are based upon enthalpies of interaction from the ab initio calculations after counterpoise and vibrational corrections have been applied. Overall, AM1 seems to do best, except for O---H…O interactions, where none of the three methods excel.     

The energetic and structural effects of single amino acid substitutions upon capped alpha-helical peptides containing 17 amino acid residues. An ONIOM DFT/AM1 study

We evaluate the effect of the amino acid mutations of glycine, leucine, valine, phenylalanine, serine, and proline for the 10th alanine in the capped peptide, acetly(Ala)(17)NH(2), upon the energies of the alpha-helices and beta-strands using ONIOM DFT/AM1 molecular orbital calculations. The relative stabilities of the alpha-helix (to the beta-strand) derive from the differences between the effects upon not only the helix but the strand as well. Thus, Ala --> Pro significantly destabilizes both but destabilizes the alpha-helix more, while Ala --> Gly stabilizes both but stabilizes the beta-strand more. The theoretical results are discussed in the context of the known experimental reports. We suggest that the solvation of the unfolded state drives the helix/coil equilibrium in solution.