对三类金属硫蛋白 (大鼠金属硫蛋白亚型II,兔肝金属硫蛋白亚型I和兔肝金属硫蛋白亚型II)的单体和二聚体进行了水溶液条件下的分子动力学模拟.其中大鼠金属硫蛋白亚型II的结构直接来自于晶体数据 ,兔肝金属硫蛋白亚型I和II的结构则通过同源蛋白模型搭建.动力学模拟的结果显示,这三种单体在水溶液中都具有相当大的柔性 ,柔性主要来源于柔性区的氨基酸残基.三类金属硫蛋白单体的动力学模拟均表明α结构域的动力学稳定性都要优于 β结构域.从主链的坐标均方根偏差可以看到,二聚体的动力学稳定性要明显优于单体 ,这主要因为在形成二聚体后柔性区域残基的构象空间受到了一定的限制. Monomers and dimers of the three classes of metallothioneins (rat metallothionein subtype II, rabbit liver metallothionein subtype I and rabbit liver metallothionein subtype II) were subjected to an aqueous solution of molecular dynamics , In which the structure of rat metallothionein subtype II is directly derived from the crystal data and the structure of rabbit hepatic metallothionein subtype I and II is established by homology protein model.The results of kinetic simulation show that the three single Body in aqueous solution has considerable flexibility, the flexibility mainly comes from the amino acid residues in the flexible region.The kinetic simulation of the three kinds of metallothionein monomers showed that the α-domain kinetic stability than the β domain From the root mean square deviation of the coordinates of the main chain, it can be seen that the kinetic stability of the dimer is significantly better than that of the monomer, mainly because the conformational space of the flexible region residues is limited after dimerization .