%0 Journal Article
%T STUDY ON UNFOLDING PROCESSES OF A SMALL PROTEIN BY MOLECULAR DYNAMICS SIMULATIONS UNDER THE COUPLING EFFECT BETWEEN PRESSURE AND TEMPERATURE<br>压强温度耦合作用下小蛋白去折叠过程的分子动力学模拟
%A Wang Ji-hua
%A Zhang Zhi-yong
%A Liu Hai-yan
%A Shi Yun-yu
%A <br>王吉华
%A 张志勇
%A 刘海燕
%A 施蕴渝
%J 生物物理学报
%D 2004
%I 
%X 56 independent molecular dynamics (MD) simulations of the B1 domain of protein G (GB1) were performed to the amount of 88.8ns under fourteen temperatures (from 280 to 540 K) and four pressures (1×102, 2×105, 5×105 and 8×105 kPa). The coupling effect between temperature and pressure during GB1 unfolding processes was studied. The stability of α helix and the β strands increased with increasing pressure. The solvent accessible surface area (SASA) and the other structural parameters decreased with increasing pressure in general. The moderate pressures such as 2×105 and 5×105 kPa restrained the unfolding rate of secondary structure of the protein by slowing down the internal motion of GB1, while higher pressures such as 8×105 kPa accelerated its unfolding rate. The cooperative exposing of the hydrophobic core of GB1 to water occurred at 1×102 and 2×105 kPa among the simulations under different temperatures, but the same phenomena did not occur at 5×105 and 8×105 kPa. The results showed that the temperature-induced unfolding process was perturbed obviously by pressure. The simulation results agree with those obtained from recent experiments.
%K Molecular dynamics simulation
%K Coupling effect between pressure and temperature
%K Unfolding process
%K GB1<br>分子动力学模拟
%K 压强温度耦合
%K 去折叠过程：GBl
%U http://www.alljournals.cn/get_abstract_url.aspx?pcid=90BA3D13E7F3BC869AC96FB3DA594E3FE34FBF7B8BC0E591&jid=E0C9D9BBED813D6674AC13E942EAC86D&aid=450B65015CF6087F&yid=D0E58B75BFD8E51C&vid=A04140E723CB732E&iid=E158A972A605785F&sid=0C3F9E980968AF79&eid=3224764AEAFCF8C2&journal_id=1000-6737&journal_name=生物物理学报&referenced_num=4&reference_num=23