The Structural Stability of Alpha-Helix Determined by the Preference of Amino Acids  

作　　者：谢潇潇 李军委 肖少英 刘玉芝 柳辉 耿金鹏 张素花 于慧 展永 安海龙 

机构地区：[1]Key Laboratory of Molecular Biophysics,Institute of Biophysics,School of Sciences,Hebei University of Technology [2]School of Architecture&Art Design,Hebei University of Technology [3]School of Electrical and Electronics Engineering,Shijiazhuang Tiedao University

出　　处：《Chinese Physics Letters》2016年第2期145-148,共4页中国物理快报（英文版）

基　　金：Supported by the National Natural Science Foundation of China under Grant Nos 11247010,11175055,11475053 and 11347017;the Natural Science Foundation for Distinguished Young Scholars of Hebei Province under Grant No C2015202340;the Natural Science Foundation of Hebei Province under Grant Nos C2012202079 and C201400305;the Scientific Innovation Fund for Excellent Young Scientists of Hebei University of Technology under Grant No 2015010

摘　　要：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.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.

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分 类 号：Q51[生物学—生物化学]