Journal
JOURNAL OF PHYSICAL CHEMISTRY A
Volume 104, Issue 11, Pages 2498-2503Publisher
AMER CHEMICAL SOC
DOI: 10.1021/jp9911189
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We examined the effect of solvation on the conformational preferences (e.g., alpha-helix versus beta-sheet) of tripeptides using ab initio quantum mechanics (Hartree-Fock 6-31G**) with solvation in the Poisson-Boltzmann continuum solvent approximation. We find that aqueous solvent preferentially stabilizes the alpha-helix conformation over beta-sheet conformations by 3.5 kcal/mol for Ala. 2.4 kcal/mol for Gly, and 2.0 kcal/mol for Pro. We determined the torsional potential surfaces of the tripeptides. Gly-Ala-Gly, Gly-Gly-Gly, and Gly-Pro-Gly using both aqueous solvent and nonpolar solvent conditions. These results were used to determine force-field torsional parameters for the protein main chains.
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