Journal
JOURNAL OF PHYSICAL CHEMISTRY B
Volume 109, Issue 18, Pages 9096-9103Publisher
AMER CHEMICAL SOC
DOI: 10.1021/jp0510692
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Funding
- NIEHS NIH HHS [T32 ES007318, ES007318] Funding Source: Medline
- NIGMS NIH HHS [R01 GM070987, F32 GM073517, GM070987] Funding Source: Medline
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We study the conformational equilibria of two peptides using, a novel statistical mechanics approach designed for calculating free energy differences between highly dissimilar conformational states. Our results elucidate the contrasting roles of entropy in implicitly solvated leucine dipeptide and decaglycine. The method extends earlier work by Voter and overcomes the notorious overlap problem in free energy computations by constructing a mathematically equivalent calculation with high conformational similarity. The approach requires only equilibrium simulations of the two states of interest, without the need for sampling transition states. We discuss possible extensions and optimizations of the approach.
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