In recent years, molecular dynamic (MD) simulations have been used to understand the effects of various processing methods on the structural properties and stability of proteins. In this study, the conformational changes in soybean trypsin inhibitor molecule were evaluated with the use of high temperature and pressure. The MD simulations have been performed at various temperatures (300 K, 345 K and 373 K) and pressure (1 bar, 3 kbar, 6 kbar) combinations. The results showed that the soybean trypsin inhibitor (STI) molecule is relatively stable at high temperatures, primarily due to the presence of disulphide bonds. However, at higher pressures, significant compaction was observed. Root mean square deviations, Radius of gyration and volume of the STI molecule were evaluated. Furthermore, Ramachandran plots were used to evaluate the stability of the various simulated molecules. It was found that the compaction resulted in high steric interferences among the core residues.

近年来，已经使用分子动力学（MD）模拟来了解各种加工方法对蛋白质的结构特性和稳定性的影响。在这项研究中，使用高温和高压评估了大豆胰蛋白酶抑制剂分子的构象变化。MD仿真是在各种温度（300 K，345 K和373 K）和压力（1 bar，3 kbar，6 kbar）组合下进行的。结果表明，大豆胰蛋白酶抑制剂（STI）分子在高温下相对稳定，这主要归因于二硫键的存在。然而，在较高的压力下，观察到明显的压实。评估均方根偏差，回转半径和STI分子的体积。此外，Ramachandran图用于评估各种模拟分子的稳定性。发现压实导致核心残基之间的高度空间干扰。