conformation transformation of aβ42 protein under different .pdf

Hans Journal of Biomedicine 生物医学, 2013, 3, 1-6 doi:10.12677/hjbm.2013.31001 Published Online January 2013 (/journal/hjbm.html) Conformation Transformation of Aβ42 Protein under * Different Temperature by Molecular Dynamics Simulations Jing Fu1,2, Liling Zhao1,3, Jihua Wang1,3# 1Shandong Provincial Key Laboratory of Functional Macromolecular Biophysics, Dezhou University, Dezhou 2College of Physics and Electronics, Shandong Normal University, Jinan 3Department of Physics, Dezhou University, Dezhou Email: fujing0203@126.com, zhaoll@, # jihuawang169@ Received: Nov. 21st th th , 2012; revised: Dec. 18 , 2012; accepted: Dec. 27 , 2012 Abstract: The temperature-induced conformation changes of Aβ42 protein were studied by molecular dynamics simu- lation. The three independent molecular dynamics simulations of Aβ42 protein at different temperatures 300 K, 340 K and 380 K, were performed using the GROMACS software package and GROMOS 43A1 force field, respectively. Each simulation was run for 60 ns. Based on the simulations, we analyzed the conformation changes of Aβ42 protein and the formation of its secondary structure and tertiary structure. The results indicated that Aβ42 protein has no stable structure and it has the characters of intrinsically disorder proteins at the different temperatures. It also shows that the structure of Aβ42 protein change obviously with different temperature. In addition, there is a change tendency from α-helix to β-sheet at 380 K. Keywords: Aβ42 Protein; Molecular Dynamics Simulation; Alzheimer’s Disease; Conformation Transformation 基于分子动力学模拟研究温度致Aβ42 蛋白构象变化* 1,2 1,3 1,3# 付静 ，赵立岭 ，王吉华 1 德州学院山东省功能大分子生物物理重点实验室，德州 2 山东师范大学物理与电子科学学院，济南 3 德州学院物理系，德州 Email: fujing0203@126.com, z