Increasing the Sampling Efficiency of Protein Conformational Change by Combining a Modified Replica Exchange Molecular Dynamics and Normal Mode Analysis-Reference-Cited by-同舟云学术

Increasing the Sampling Efficiency of Protein Conformational Change by Combining a Modified Replica Exchange Molecular Dynamics and Normal Mode Analysis

Published:2020-12-22 Issue:1 Volume:17 Page:13-28
ISSN:1549-9618
Container-title:Journal of Chemical Theory and Computation
language:en
Short-container-title:J. Chem. Theory Comput.

Author:

Peng Cheng¹²,Wang Jinan¹,Shi Yulong¹²,Xu Zhijian¹²^ORCID,Zhu Weiliang¹³²^ORCID

Affiliation:

1. CAS Key Laboratory of Receptor Research; Drug Discovery and Design Center, Shanghai Institute of Materia Medica, Chinese Academy of Sciences, 555 Zuchongzhi Road, Shanghai, 201203, China

2. University of Chinese Academy of Sciences, No.19A Yuquan Road, Beijing, 100049, China

3. Open Studio for Druggability Research of Marine Lead Compounds, Qingdao National Laboratory for Marine Science and Technology, 1 Wenhai Road, Aoshanwei, Jimo, Qingdao 266237, China

Funder

Ministry of Science and Technology of the People's Republic of China

National Natural Science Foundation of China

Publisher

American Chemical Society (ACS)

Subject

Physical and Theoretical Chemistry,Computer Science Applications

Link

https://pubs.acs.org/doi/pdf/10.1021/acs.jctc.0c00592

Reference124 articles.

1. The nature of protein folding pathways

2. Accelerated molecular dynamics simulations of ligand binding to a muscarinic G-protein-coupled receptor