%0 Journal Article
%T EFFECTS OF ELECTROSTATIC AND HYDROPHOBIC INTERACTIONON THE STABILITY OF INSULIN DIMER<br>静电和疏水效应对胰岛素二聚体稳定性的影响
%A MA Xiao-hui
%A CHEN Wei-zu
%A ZHUANG Yan
%A WANG Cun-xin
%A HOU Ting-jun
%A QIAO Xue-bing
%A XU Xiao-jie
%A <br>马晓慧
%A 陈慰祖
%A 庄彦
%A 王存新
%A 侯廷军
%A 乔学兵
%A 徐筱杰
%J 生物物理学报
%D 2001
%I 
%X 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.
%K Insulin dimer
%K Molecular interface
%K Electrostatic interactions
%K Hydrophobic effects<br>胰岛素二体
%K 分子表面
%K 静电作用
%K 疏水作用
%K 稳定性
%U http://www.alljournals.cn/get_abstract_url.aspx?pcid=90BA3D13E7F3BC869AC96FB3DA594E3FE34FBF7B8BC0E591&jid=E0C9D9BBED813D6674AC13E942EAC86D&aid=C7A4264930B88EF0&yid=14E7EF987E4155E6&vid=BCA2697F357F2001&iid=0B39A22176CE99FB&sid=C6EC7357BCACD3A4&eid=50EA2A80A7D254EF&journal_id=1000-6737&journal_name=生物物理学报&referenced_num=2&reference_num=13