【摘要】 从猪胰岛素二聚体的结构出发 ,着重研究了胰岛素二聚体单体之间的静电和疏水相互作用 ,用连续介质模型的有限差分方法计算得到胰岛素二聚体的静电势 ,用溶剂可接近表面 (ASA)模型分析了分子表面积及疏水性 ,还考察了不同pH值对胰岛素二聚体静电和疏水相互作用的影响。结果分析表明 ,当pH值处于弱酸弱碱范围内时 (4.6 -8.5) ,静电相互作用能和疏水自由能都呈现出较小的值 ,当pH为6.2时 ,疏水性出现一个明显的峰值 ,这与猪胰岛素二聚体结晶的实验条件相吻合。更多还原

【Abstract】 The crystal structure of the pig insulin dimer (4ins) was used to study the electrostatic and hydrophobic interactions between two monomers. The Continuum model and the finite difference Poisson-Boltzmann (FDPB) method were used to calculate the electrostatic potentials of the system. The molecular surface was explored in the condition of different pH values. The results indicate that the electrostatic interaction energy and the desolvation free energy show smaller values when pH values are between 4.6 and 8.5. The hydrophobicity denotes an obvious peak when pH is near 6.2. These results are consistent with the experimental condition for insulin dimer crystallization.更多还原