Chin. Phys. Lett.  2016, Vol. 33 Issue (02): 028701    DOI: 10.1088/0256-307X/33/2/028701
CROSS-DISCIPLINARY PHYSICS AND RELATED AREAS OF SCIENCE AND TECHNOLOGY |
The Structural Stability of Alpha-Helix Determined by the Preference of Amino Acids
Xiao-Xiao Xie1‡, Jun-Wei Li1‡, Shao-Ying Xiao2, Yu-Zhi Liu3, Hui Liu1, Jin-Peng Geng1, Su-Hua Zhang1, Hui Yu1, Yong Zhan1**, Hai-Long An1**
1Key Laboratory of Molecular Biophysics, Institute of Biophysics, School of Sciences, Hebei University of Technology, Tianjin 300401
2School of Architecture & Art Design, Hebei University of Technology, Tianjin 300401
3School of Electrical and Electronics Engineering, Shijiazhuang Tiedao University, Shijiazhuang 050043
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Xiao-Xiao Xie, Jun-Wei Li, Shao-Ying Xiao et al  2016 Chin. Phys. Lett. 33 028701
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Abstract To accomplish their functions, proteins have to achieve different conformations accompanied by conformational transitions. However, the relationship between the preference of amino acids and the stability of the secondary structure is still unclear. Here we perform molecular simulations on a series of helical structures. Our data show that the dissociation energy of the helical structure is related to the preference of amino acids, and the electrostatic repulsion of the residue $i$ and $i+3/4$ with the same sign of charge destabilizes the alpha helix.
Received: 27 July 2015      Published: 26 February 2016
PACS:  87.15.hp (Conformational changes)  
  87.15.ap (Molecular dynamics simulation)  
  87.16.Vy (Ion channels)  
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https://cpl.iphy.ac.cn/10.1088/0256-307X/33/2/028701       OR      https://cpl.iphy.ac.cn/Y2016/V33/I02/028701
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Xiao-Xiao Xie
Jun-Wei Li
Shao-Ying Xiao
Yu-Zhi Liu
Hui Liu
Jin-Peng Geng
Su-Hua Zhang
Hui Yu
Yong Zhan
Hai-Long An
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