Multi-scale molecular dynamics simulations and applications on mechanosensitive proteins of integrins

• Published in: Chinese physics B Vol. 30; no. 3; pp. 38701 - 8
• Main Authors: Lü, Shouqin, Ding, Qihan, Zhang, Mingkun, Long, Mian
• Format: Journal Article
• Language: English
• Published: School of Engineering Science,University of Chinese Academy of Sciences,Beijing 101408,China 01.03.2021; Chongqing Engineering Research Center of High-Resolution and 3D Dynamic Imaging Technology,Chongqing Institute of Green and Intelligent Technology,Chinese Academy of Sciences,Chongqing 400714,China; Center of Biomechanics and Bioengineering,Key Laboratory of Microgravity(National Microgravity Laboratory),Beijing Key Laboratory of Engineered Construction and echanobiology,and CAS Center for Excellence in Complex System chanics,Institute of Mechanics,Chinese Academy of Sciences(CAS),Beijing 00190,China; School of Engineering Science,University of Chinese Academy of Sciences,Beijing 101408,China%Center of Biomechanics and Bioengineering,Key Laboratory of Microgravity(National Microgravity Laboratory),Beijing Key Laboratory of Engineered Construction and echanobiology,and CAS Center for Excellence in Complex System chanics,Institute of Mechanics,Chinese Academy of Sciences(CAS),Beijing 00190,China
• Subjects: molecular dynamics simulations; integrin; mechanosensitive protein; allosteric dynamics
• ISSN: 1674-1056; 2058-3834
• DOI: 10.1088/1674-1056/abc540

Molecular dynamics simulation (MDS) is a powerful technology for investigating evolution dynamics of target proteins, and it is used widely in various fields from materials to biology. This mini-review introduced the principles, main preforming procedures, and advances of MDS, as well as its applications on the studies of conformational and allosteric dynamics of proteins especially on that of the mechanosensitive integrins. Future perspectives were also proposed. This review could provide clues in understanding the potentiality of MD simulations in structure–function relationship investigation of biological proteins.