Developing a molecular dynamics force field for both folded and disordered protein states
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- Paul Robustelli
- D. E. Shaw Research, New York, NY 10036;
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- Stefano Piana
- D. E. Shaw Research, New York, NY 10036;
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- David E. Shaw
- D. E. Shaw Research, New York, NY 10036;
書誌事項
- 公開日
- 2018-05-07
- 権利情報
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- https://creativecommons.org/licenses/by-nc-nd/4.0/
- DOI
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- 10.1073/pnas.1800690115
- 公開者
- Proceedings of the National Academy of Sciences
この論文をさがす
説明
<jats:title>Significance</jats:title> <jats:p>Many proteins that perform important biological functions are completely or partially disordered under physiological conditions. Molecular dynamics simulations could be a powerful tool for the structural characterization of such proteins, but it has been unclear whether the physical models (force fields) used in simulations are sufficiently accurate. Here, we systematically compare the accuracy of a number of different force fields in simulations of both ordered and disordered proteins, finding that each force field has strengths and limitations. We then describe a force field that substantially improves on the state-of-the-art accuracy for simulations of disordered proteins without sacrificing accuracy for folded proteins, thus broadening the range of biological systems amenable to molecular dynamics simulations.</jats:p>
収録刊行物
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- Proceedings of the National Academy of Sciences
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Proceedings of the National Academy of Sciences 115 (21), E4758-, 2018-05-07
Proceedings of the National Academy of Sciences
