Molecular dynamics simulation of the interaction between the Tenebrio molitor alpha-amylase and its inhibitor at different proportion of crystal water was carried out with OPLS force field by hyperchem 7.5 software. In the correlative study, the optimal temperature of wheat monomeric and dimeric protein inhibitors was from 273 K to 318 K. The the average temperature of experimentation is 289 K. (1) The optimal temperature of interaction between alpha-amylase and its inhibitors was 280 K without crystal water that was close to the results of experimentation. The forming of enzyme-water and inhibitor-water was easy, but incorporating third monomer was impossible. (2) Having analyzed the potential energy data, the optimal temperature of interaction energy between alpha-amylase and its inhibitors covering 9 : 1, 5 : 5, 4 : 6, and 1 : 9 proportion crystal water was 290 K. (3) We compared the correlative QSAR properties. The proportion of crystal water was close to the data of polarizability (12.4%) in the QSAR properties. The optimal temperature was 280 K. This result was close to 289 K. These findings have theoretical and practical implications.

中文翻译：

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结晶水影响黄粉虫α-淀粉酶与其抑制剂之间的相互作用。

黄粉虫α-淀粉酶与其抑制剂在不同结晶水比例下相互作用的分子动力学模拟采用OPLS力场，通过hyperchem 7.5软件进行。在相关研究中，小麦单体和二聚体蛋白抑制剂的最适温度为273 K～318 K。实验平均温度为289 K。 (1) α-淀粉酶与其抑制剂相互作用的最适温度为280 K 无结晶水，接近实验结果。酶水和抑制剂水的形成很容易，但不可能掺入第三单体。(2) 分析了势能数据，α-淀粉酶与其抑制剂相互作用能的最适温度包括9：1、5：5、4：6和1：9 比例的结晶水为 290 K。 (3) 我们比较了相关的 QSAR 特性。结晶水的比例接近QSAR特性中的极化率数据（12.4%）。最佳温度为 280 K。该结果接近 289 K。这些发现具有理论和实践意义。