Based on three-dimensional structural information of protein, solvent accessible surface area and network properties were calculated. 其次根据蛋白质的三维结构计算得到氨基酸的溶剂可及化表面积和蛋白质的残基相互作用网络参数。
The solvent accessible surface area, local dipole moments and surface electrostatic feild of amino acids have been calculated. 我们计算了氨基酸的溶剂可接近面积,局域偶极矩及表面电场。
We made full use of the protein sequence and structure information, namely, physical and chemical properties, evolution information and solvent accessible surface area. 建立预测模型过程中,我们充分考虑了蛋白质的序列信息和结构信息,即蛋白质的物理化学性质、进化信息以及溶剂可及化表面积。
Solvent accessible surface area, cavity numbers and volume, compactness, hydrophobicity and temperature factor are the major three-dimension structural parameters that contribute to protein thermostability. 溶剂接触表面积、空腔个数和体积、紧密度、疏水性以及温度因子是影响蛋白质耐热的主要三维结构参数。
Solving the Poisson-Boltzmann equation the finite difference method was used to calculate the electrostatic potential. The solvent accessible surface model was supplied for the molecular surface and hydrophobicity. 蛋白质的静电相互作用通过有限差分方法求解Poisson-Boltzmann方程得到,疏水相互作用通过分析溶剂可及性表面模型得到。