从 1995年以前的蛋白质数据库中选出了 3 7套不同酶的晶体学数据 ,分别对其活性部位关键残基和整个分子的晶体学温度因子 (B)进行了统计分析 .结果显示 ,3 7种酶中有 2 6种酶的活性部位关键残基相对于分子整体而言具有较低的B因子 ,只有 7种较高 .这表明 ,在晶体状态下 ,大多数天然酶的活性部位关键残基可能具有比分子整体更稳定的构象 .对酶活性部位在变性剂的作用下表现出柔性的原因进行了讨论 . A total of 37 crystallographic data of different enzymes were selected from the protein database before 1995 and the crystallographic temperature factors (B) of the key residues in the active site and the whole molecule were analyzed respectively. The results showed that 37 There are 26 kinds of enzymes in the enzyme active site of the key residues relative to the overall molecule has a lower B factor, only 7 higher.This shows that in the crystal state, most of the natural enzyme active site key residues The base may have a more stable conformation than the entire molecule, and the reason why the active site of the enzyme exhibits flexibility under the action of a denaturing agent is discussed.