从胰岛素研究看等构相互作用在分子识别中的作用

摘要

The structural basis of molecular recognition in proteins is the specific three dimensional structure or folding of the proteins, the information for which is contained in the sequence. When the structural homology of proteins with known or unknown functions are compared, it is an usual way to base such comparisons on the hydrophobicity or hydrophilicity of the amino acid residues. Studies on insulin by site directed mutagenesis reveal the importance of "isosteric interaction" in considering the possible protein homology. With the concept of "isosteric interaction" in mind there will be more to consider for the structure and function studies on proteins and more choices for the preparation of peptide and protein analogues or mimetics in pharmaceutical industry.%蛋白质分子识别的结构基础是蛋白质的三维结构或折叠,其信息存在于氨基酸序列中.在比较功能已知或未知蛋白质的结构同源性时,常常是根据氨基酸残基的疏水性或亲水性.胰岛素定位突变的研究显示出了"等构相互作用"#在考虑蛋白质同源性中的重要性."等构相互作用"这一概念使得蛋白质结构与功能研究的视野更加开阔,同时在制药工业中开发多肽与蛋白质的类似物或模拟物有更多的选择.