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.
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
