Sampling of Protein Folding Transitions: Multicanonical Versus Replica Exchange Molecular Dynamics.
Sampling of Protein Folding Transitions: Multicanonical Versus Replica Exchange Molecular Dynamics.
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DOI：
10.1021/ct400312d
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发表时间：
2013-08-13
影响因子：
5.5
通讯作者：
Hansmann, Ulrich H. E.
中科院分区：
文献类型：
--
作者：
Jiang, Ping;Yasar, Fatih;Hansmann, Ulrich H. E.
We compare the efficiency of multicanonical and replica exchange molecular dynamics for the sampling of folding/unfolding events in simulations of proteins with end-to-end β-sheet. In Go-model simulations of the 75-residue MNK6, we observe improvement factors of 30 in the number of folding/unfolding events of multicanonical molecular dynamics over replica exchange molecular dynamics. As an application, we use this enhanced sampling to study the folding landscape of the 36-residue DS119 with an all-atom physical force field and implicit solvent. Here, we find that the rate-limiting step is the formation of the central helix that then provides a scaffold for the parallel β-sheet formed by the two chain ends.
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影响因子：
5.5
作者：
Hess, Berk;Kutzner, Carsten;Lindahl, Erik
通讯作者：
Lindahl, Erik
影响因子：
2.8
作者：
Hansmann, UHE
通讯作者：
Hansmann, UHE
DOI：
10.1080/01621459.1995.10476590
发表时间：
1995-09-01
影响因子：
3.7
作者：
GEYER, CJ;THOMPSON, EA
通讯作者：
THOMPSON, EA
影响因子：
5.5
作者：
Hess, Berk
通讯作者：
Hess, Berk
影响因子：
5.5
作者：
Jiang, Ping;Hansmann, Ulrich H. E.
通讯作者：
Hansmann, Ulrich H. E.