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On the Transferability of CHARMM36m Protein Force Field with LJ-PME: Hydrogen Bonding Dynamics under Elevated Pressures

29 January 2021, Version 1
Working Paper
This content is a preprint and has not undergone peer review at the time of posting.

Abstract

The pressure-temperature phase diagram is significant to understanding the physics of biomolecules. In this study we evaluated the transferability of CHARMM36m (C36m) protein force field (FF) in varied pressures using ubiquitin as a model protein compared with NMR data. We demonstrate that C36m FF combining with the LJ-PME method is suitable for simulations in a wide range of temperature and pressure.

Keywords

molecular simulation
protein force field
CHARMM36m
LJ-PME
ubiquitin

Supplementary materials

Title
Description
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Title
manuscript-ubi.v6
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Version History

Jan 29, 2021 Version 1

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The content is available under CC BY NC ND 4.0 [opens in a new tab]

DOI

10.26434/chemrxiv.13653203.v1
D O I: 10.26434/chemrxiv.13653203.v1 [opens in a new tab]

Funding

LR19B030001 | Zhejiang Provincial Natural Science Foundation of China
LQ20C05001 | Zhejiang Provincial Natural Science Foundation of China
National Natural Science Foundation of China
21803057
Study on the conformational ensemble and self-assembly of natural disordered proteins using polarizable molecular force fields
https://app.dimensions.ai/details/grant/grant.8900365 [opens in a new tab]

Author’s competing interest statement

no conflict of interest

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