ScholarWorks@숙명여자대학교

초록

Accurate estimation of conformational entropy for complex biomolecules remains a challenge in chemical physics. The most popular quasiharmonic method assumes a multivariate Gaussian distribution of protein structural fluctuations, while a recently proposed energetic approach assumes a Gaussian distribution of the solvent-averaged effective energy. Here we examine the fundamental assumptions in these approaches, and demonstrate that the conventional structural approach yields unreliable estimate of conformational entropy due to inherent anharmonicities associated with the presence of multiple local energy wells, whereas the energetic approach retains efficacy since those energy wells sample similar values of the effective energy. (C) 2015 Elsevier B.V. All rights reserved.

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