耐热碱性磷酸酶(FD-TAP)的结构模型研究

 以大肠杆菌碱性磷酸酶 (BAP)为主要结构模板 ,用计算机同源结构模拟方法构建了耐热碱性磷酸酶 (FD TAP)的三维结构 ,对它们的结构特征进行了分析比较 ,并用Profile 3D和Ramachand ran图等方法分析了结构的合理性 .在此基础上 ,又构建了FD TAP 3个突变体的结构 ,用CHARMM能量计算法研究了FD TAP及其 3个突变体的能量与酶蛋白热稳定性之间的关系 ,得到了与实验完全一致的结果 .结果说明 ,如果氨基酸残基置换使蛋白质分子的总能量降低 ,疏水性增高和柔韧性减小 ,往往使蛋白质的耐热性增加

Modeling Study of the Thermostable Alkaline Phosphatase(FD-TAP)

The 3D structure of thermostable alkaline phosphatase(FD\|TAP) was modeled based on the known X\|ray structure of Escherichia coli alkaline phosphatase (BAP),using homology modeling.The rationality of resulting model of FD\|TAP was validated by Ramanchandran plot and Profile\|3D.On this basis,the three mutants of FD\|TAP were modeled,the relationship between the energy and the thermostability of the FD\|TAP and its mutants was studied by CHARMM energy.The result corresponds well with the experiments.It suggests that the decrease of the total energy and flexibility and increase of hydrophobicity of the protein by substitution of amino acids result in the increase of the thermostability.