Predicting Protein-Protein Interaction Sites from Sequence Profile and Accessible Surface Area(ASA) 基于序列剖面和可及表面积的蛋白质相互作用位点的预测
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。
And the nonpolar solvation energy is often obtained from the solvent - accessible surface area ( SA ). 溶液效应中非极性部分对自由能的贡献则通过分子表面积(SA)计算得到。