Mapping Central α-Helix Linker Mediated Conformational Transition Pathway of Calmodulin via Simple Computational Approach-Reference-Cited by-同舟云学术

Mapping Central α-Helix Linker Mediated Conformational Transition Pathway of Calmodulin via Simple Computational Approach

Published:2014-08-05 Issue:32 Volume:118 Page:9677-9685
ISSN:1520-6106
Container-title:The Journal of Physical Chemistry B
language:en
Short-container-title:J. Phys. Chem. B

Author:

Wang Jinan¹,Peng Shaoliang²,Cossins Benjamin P.³,Liao Xiangke²,Chen Kaixian¹,Shao Qiang¹,Zhu Xiaoqian²,Shi Jiye³,Zhu Weiliang¹

Affiliation:

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

2. School of Computer Science & State Key Laboratory of High Performance Computing, National University of Defense Technology, No. 47, Yanwachi Street, Kaifu District, Changsha, Hunan 410073, China

3. UCB Pharma, 216 Bath Road, Slough SL1 4EN, United Kingdom

Funder

National Natural Science Foundation of China

National 863 Program

Publisher

American Chemical Society (ACS)

Subject

Materials Chemistry,Surfaces, Coatings and Films,Physical and Theoretical Chemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/jp507186h

Reference48 articles.

1. The intrinsic dynamics of enzymes plays a dominant role in determining the structural changes induced upon inhibitor binding