期刊
EUROPEAN BIOPHYSICS JOURNAL WITH BIOPHYSICS LETTERS
卷 40, 期 7, 页码 843-856出版社
SPRINGER
DOI: 10.1007/s00249-011-0700-9
关键词
GROMOS; 54A7; Force field; Secondary structure
类别
资金
- National Center of Competence in Research (NCCR) in Structural Biology
- Swiss National Science Foundation [200020-121913]
- European Research Council [228076]
- Australian Research Council [DP0770375]
- Australian Research Council [DP0770375] Funding Source: Australian Research Council
New parameter sets of the GROMOS biomolecular force field, 54A7 and 54B7, are introduced. These parameter sets summarise some previously published force field modifications: The 53A6 helical propensities are corrected through new phi/psi torsional angle terms and a modification of the N-H, C=O repulsion, a new atom type for a charged -CH3 in the choline moiety is added, the Na+ and Cl- ions are modified to reproduce the free energy of hydration, and additional improper torsional angle types for free energy calculations involving a chirality change are introduced. The new helical propensity modification is tested using the benchmark proteins hen egg-white lysozyme, fox1 RNA binding domain, chorismate mutase and the GCN4-p1 peptide. The stability of the proteins is improved in comparison with the 53A6 force field, and good agreement with a range of primary experimental data is obtained.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据