胰蛋白酶活性中心Asp-102、His-57和Ser-195残基的构象  

Conformations of the Trypsin Active Center Asp-102,His-57 and Ser-195 Residues

作　　者：付继军[1] 李映苓[1] 邱开雄[1] 简虹[1] 黄大荣[1] 

机构地区：[1]昆明医学院化学教研室,昆明650031

出　　处：《昆明医学院学报》2005年第4期24-26,共3页Journal of Kunming Medical College

摘　　要：目的:分析胰蛋白酶活性中心Asp-102、His-57和Ser-195残基的构象与催化之关系.方法:用半经验的构象分析法计算胰蛋白酶的约含800个原子的活性中心场中Asp-102、His-57和Ser-195催化三联体侧链的最低能量状态.结果:在胰蛋白酶的结构中,孤立残基构成优势构象,侧链的柔性与酶的催化功能相符.结论:半经验的构象分析法计算结果与用X-线结构分析胰蛋白酶复合物所得资料相一致.Objective： To explore the low energetic conformations of trypsin＇s catalytic triad Asp- 102, His- 57, Ser- 195 in the field of the.active center that consisted of about 800 atoms. Methods： Conformational analysis. Results： It was shown that within the enzyme structure conformations which were preferential for imlated residues were formed. Lability obtained for the side chains is in accord with the functions in enzymatic catalysis. Conclusion： Results of the calculations carried out correlate with the X- ray data for trypsin complex.

关 键 词：胰蛋白酶活性中心 构象 分析 

分 类 号：Q641.6[生物学—生物物理学]