期刊
PHYSICAL REVIEW LETTERS
卷 98, 期 4, 页码 -出版社
AMERICAN PHYSICAL SOC
DOI: 10.1103/PhysRevLett.98.048102
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The near-native free-energy landscape of protein G is investigated through 0.4-mu s-long atomistic molecular dynamics simulations in an explicit solvent. A theoretical and computational framework is used to assess the time dependence of salient thermodynamical features. While the quasiharmonic character of the free energy is found to degrade in a few ns, the slow modes display a very mild dependence on the trajectory duration. This property originates from a striking self-similarity of the free-energy landscape embodied by the consistency of the principal directions of the local minima, where the system dwells for several ns, and of the virtual jumps connecting them.
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