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为了研究嗜盐酶如何在高盐环境下维持稳定性与活性,本文以沃尔卡尼极嗜盐菌及大肠杆菌的二氢叶酸还原酶(DHFR)为模型,将二者分别置于5种不同盐浓度的水溶液中进行分子动力学模拟。经9ns动力学模拟,得到了二者在不同浓度盐溶液中的运动轨迹,通过对运动轨迹的分析,获取了二者在不同盐浓度下的动力学特性。结果发现嗜盐古生菌的二氢叶酸还原酶自身所形成盐桥及与溶剂所形成的氢键均比大肠杆菌的二氢叶酸还原酶多,而溶剂可及性表面则要小,二者差异均达极显著水平。同时还分析了这两种分子及其氨基酸残基的柔性等。
In order to study how halophilic enzymes can maintain their stability and activity under high salt environment, the models of diarrhea folate reductase (DHFR) from Volkan and halophilic bacteria and Escherichia coli Different salt concentrations in aqueous solution for molecular dynamics simulation. After 9ns dynamic simulation, the kinematic trajectories of the two in salt solutions with different concentrations were obtained. By analyzing the trajectories, the kinetic properties of the two solutions at different salt concentrations were obtained. The results showed that dihydrofolate reductase of halophilic archaea formed salt bridge itself and formed hydrogen bonds with the solvent more than dihydrofolate reductase of E. coli, while the solvent accessibility surface was smaller, both The differences reached extremely significant level. At the same time also analyzed the flexibility of these two molecules and their amino acid residues.