溶剂化
化学
三肽
溶剂
从头算
水溶液
计算化学
溶剂效应
分子力学
结晶学
物理化学
分子动力学
肽
有机化学
生物化学
作者
Changmoon Park,M. Carlson,William A. Goddard
摘要
We examined the effect of solvation on the conformational preferences (e.g., α-helix versus β-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 α-helix conformation over β-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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