CHARMM36m: An improved force field for folded and intrinsically disordered proteins

被引：0
|
作者：
Huang J. [1 ]
Rauscher S. [2 ]
Nawrocki G. [3 ]
Ran T. [1 ]
Feig M. [3 ]
De Groot B.L. [2 ]
Grubmüller H. [2 ]
MacKerell A.D., Jr. [1 ]
机构：
[1] Department of Pharmaceutical Sciences, School of Pharmacy, University of Maryland, Baltimore, MD
[2] Department of Theoretical and Computational Biophysics, Max Planck Institute for Biophysical Chemistry, Göttingen
[3] Department of Biochemistry and Molecular Biology, Michigan State University, East Lansing, MI
来源：
Nature Methods | 2017年 / 14卷 / 1期
基金：
美国国家卫生研究院;
关键词：
D O I：
10.1038/nmeth.4067
中图分类号：
学科分类号：
摘要：
The all-atom additive CHARMM36 protein force field is widely used in molecular modeling and simulations. We present its refinement, CHARMM36m (http://mackerell.umaryland.edu/charmm-ff.shtml), with improved accuracy in generating polypeptide backbone conformational ensembles for intrinsically disordered peptides and proteins. © 2017 Nature America, Inc., part of Springer Nature. All rights reserved.
引用
收藏
页码：71 / 73
页数：2
相关论文
共 50 条
  • [1] CHARMM36m: an improved force field for folded and intrinsically disordered proteins
    Huang, Jing
    Rauscher, Sarah
    Nawrocki, Grzegorz
    Ran, Ting
    Feig, Michael
    de Groot, Bert L.
    Grubmueller, Helmut
    MacKerell, Alexander D., Jr.
    NATURE METHODS, 2017, 14 (01) : 71 - 73
  • [2] CHARMM36: An Improved Force Field for Folded and Intrinsically Disordered Proteins
    Huang, Jing
    Rauscher, Sarah
    Nawrocki, Grzegorz
    Ran, Ting
    Feig, Michael
    de Groot, Bert L.
    Grubmueller, Helmut
    MacKerell, Alexander D., Jr.
    BIOPHYSICAL JOURNAL, 2017, 112 (03) : 175A - 176A
  • [3] Extensive tests and evaluation of the CHARMM36IDPSFF force field for intrinsically disordered proteins and folded proteins
    Liu, Hao
    Song, Dong
    Zhang, Yangpeng
    Yang, Sheng
    Luo, Ray
    Chen, Hai-Feng
    PHYSICAL CHEMISTRY CHEMICAL PHYSICS, 2019, 21 (39) : 21918 - 21931
  • [4] Performance of CHARMM36m with modified water model in simulating intrinsically disordered proteins:a case study
    Laura I.Gil Pineda
    Laurie N.Milko
    Yi He
    Biophysics Reports, 2020, 6(Z1) (Z1) : 80 - 87
  • [5] Improved conformational sampling of intrinsically disordered proteins with the modified CHARMM36 protein force field
    Huang, Jing
    Mackerell, Alexander
    ABSTRACTS OF PAPERS OF THE AMERICAN CHEMICAL SOCIETY, 2016, 252
  • [6] Improving the CHARMM36m force field for arginine-phosphate interactions
    Min, Jiyeon
    Britt, Madolyn
    Sukharev, Sergei I.
    Brooks, Bernard R.
    Klauda, Jeffery B.
    BIOPHYSICAL JOURNAL, 2023, 122 (03) : 184A - 184A
  • [7] Intrinsically disordered protein-specific force field CHARMM36IDPSFF
    Liu, Hao
    Song, Dong
    Lu, Hui
    Luo, Ray
    Chen, Hai-Feng
    CHEMICAL BIOLOGY & DRUG DESIGN, 2018, 92 (04) : 1722 - 1735
  • [8] Evaluation of the CHARMM36m force field combined with the OPC water model for protein simulations
    Kozlowski, Nicolai
    Nagy, Gabor
    Grubmuller, Helmut
    BIOPHYSICAL JOURNAL, 2023, 122 (03) : 421A - 421A
  • [9] Exploring the effectiveness of the CHARMM36m force field in depicting arginine-phosphate interactions
    Min, Jiyeon
    Britt, Madolyn
    Sukharev, Sergei I.
    Brooks, Bernard R.
    Klauda, Jeffery B.
    BIOPHYSICAL JOURNAL, 2024, 123 (03) : 473A - 474A
  • [10] Extending the Stochastic Titration CpHMD to CHARMM36m
    Sequeira, Joao G. N.
    Rodrigues, Filipe E. P.
    Silva, Telmo G. D.
    Reis, Pedro B. P. S.
    Machuqueiro, Miguel
    JOURNAL OF PHYSICAL CHEMISTRY B, 2022, 126 (40): : 7870 - 7882
12345