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为了研究嗜热酶、嗜冷酶在极端温度下维持稳定性和活性的机制,本文通过分子动力学模拟的方法,从原子尺度上分析了嗜热苹果酸脱氢酶及其同源嗜冷酶的分子动力学特性。数据显示嗜热酶所形成的盐桥和氢键明显多于嗜冷酶。通过比较均方根偏差、回旋半径、氨基酸残基的柔性等值,发现嗜热酶的结构较非嗜热酶更具刚性。盐桥、氢键数目的不同和整体结构的刚柔性,很可能会是嗜热、嗜冷酶在极端温度下能维持结构稳定的主要原因。
In order to study the mechanisms of thermophilic enzymes and psychrophilic enzymes in maintaining stability and activity at extreme temperatures, the thermophilic malate dehydrogenase and its homophilic psychrophilic enzymes were analyzed on an atomic scale by molecular dynamics simulation Molecular dynamics. The data show that the salt bridges and hydrogen bonds formed by thermophilic enzymes are significantly more than those of psychrophilic enzymes. By comparing rms deviations, gyration radii, and flexibility of amino acid residues, the structure of thermophilic enzyme was found to be more rigid than non-thermophilic enzyme. Salt bridges, the different number of hydrogen bonds, and the rigidity and flexibility of the overall structure are likely to be the main cause of thermophilic and psychrophilic enzymes that remain structurally stable at extreme temperatures.