Monte Carlo Determination of the Free Energy and Internal Energy of Hydration for the Ala Dipeptide at 25 °C

M. Mezei, P. K. Mehrotra, D. L. Beveridge

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Abstract

The differences in the free energy and internal energy of hydration of the Ala dipeptide in the C7, αR, C5, and PII conformations were computed with the Monte Carlo method in the (T, V, N) ensemble at 25 °C. The free-energy differences were obtained by determining the relative probabilities of the conformations that lie on a line that connects two conformations in the (ψ, ϕ) torsion angle space. The determination of one free-energy difference required three to five separate Monte Carlo runs using non-Boltzman sampling. The results indicate that both the αR and PIIconformations are preferentially stabilized by hydration. The major contributing factor for the stability of internal energy of hydration for these conformations can be traced to the hydration of the carbonyl group.

Original languageEnglish
Pages (from-to)2239-2245
Number of pages7
JournalJournal of the American Chemical Society
Volume107
Issue number8
DOIs
StatePublished - 1985
Externally publishedYes

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