期刊
JOURNAL OF CHEMICAL THEORY AND COMPUTATION
卷 15, 期 1, 页码 7-12出版社
AMER CHEMICAL SOC
DOI: 10.1021/acs.jctc.8b00839
关键词
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资金
- UNINETT Sigma2 - the National Infrastructure for High Performance Computing and Data Storage in Norway [4700k]
- Norwegian Research Council (FRIMEDBIO) [214167, 251247]
- National Institutes of Health [GM070855, GM072558]
Cation-pi interactions between tryptophan and choline or trimethylated lysines are vital for many biological processes. The performance of the additive CHARMM36 force field against target quantum mechanical data is shown to reproduce QM equilibrium geometries but required modified Lennard-Jones potentials to accurately reproduce the QM interaction energies. The modified parameter set allows accurate modeling, including free energies, of cation-pi indole-choline and indole-trimethylated lysines interactions relevant for protein-ligand, protein membrane, and protein-protein interfaces.
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