Comparison in structural stability between chain A and B of CLC-ec 1 exchanger by using MD simulatio
The CLC-type exchangers have been extensively studied in recent years. CLC-ecl, whose crystal structure is known and several experimental and theoretical hot spots have been identified, but the structural stability in true solution environment of this protein has not been provided. In this paper, we analyzed the structural stability of CLC-ecl protein by using the atomistic molecular dynamics (MD) simulation. The simulation result indicates that there exists no inevitable correlation between chain A and chain B in expressing their biological function. Chain A has smaller average Cα displacement value than that of chain B. The calculated electrostatic binding free energy and its fluctuation of chain A are also smaller. These results indicate that chain A has more stable structure than chain B in physical essence. It is to say that chain A may be more reliable than chain B in expressing their biological function. This work proposes a new topic on future experimental and theoretical investigations for biologists and biophysicists.
protein molecular dynamics chloride channel
Tao Yu Chun-Xu Pan Jian-Ping Sang Xian-Wu Zou
Department of Physics Wuhan University Wuhan 430072, China Department of Physics Jianghan University Department of Physics Wuhan University Wuhan 430072, China
国际会议
上海
英文
1837-1840
2011-10-15（万方平台首次上网日期，不代表论文的发表时间）