AMOEBA+ Classical Potential for Modeling Molecular Interactions-Reference-Cited by-同舟云学术

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AMOEBA+ Classical Potential for Modeling Molecular Interactions

Published:2019-05-28 Issue:7 Volume:15 Page:4122-4139
ISSN:1549-9618
Container-title:Journal of Chemical Theory and Computation
language:en
Short-container-title:J. Chem. Theory Comput.

Author:

Liu Chengwen¹^ORCID,Piquemal Jean-Philip¹²³^ORCID,Ren Pengyu¹

Affiliation:

1. Department of Biomedical Engineering, The University of Texas at Austin, Austin, Texas 78712, United States

2. Laboratoire de Chimie Théorique, Sorbonne Université, UMR7616 CNRS, Paris 75252, France

3. Institut Universitaire de France, Paris Cedex 05, 75005, France

Funder

National Institute of General Medical Sciences

Publisher

American Chemical Society (ACS)

Subject

Physical and Theoretical Chemistry,Computer Science Applications

Link

https://pubs.acs.org/doi/pdf/10.1021/acs.jctc.9b00261

Reference132 articles.

1. ff14SB: Improving the Accuracy of Protein Side Chain and Backbone Parameters from ff99SB

2. Further along the Road Less Traveled: AMBER ff15ipq, an Original Protein Force Field Built on a Self-Consistent Physical Model

3. Building a More Predictive Protein Force Field: A Systematic and Reproducible Route to AMBER-FB15

4. An overview of the Amber biomolecular simulation package

5. All-Atom Empirical Potential for Molecular Modeling and Dynamics Studies of Proteins

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4. A Polarizable QM/MM Model That Combines the State-Averaged CASSCF and AMOEBA Force Field for Photoreactions in Proteins;Journal of Chemical Theory and Computation;2024-08-01

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