Key role of proximal water in regulating thermostable proteins.
Key role of proximal water in regulating thermostable proteins.
复制标题
近端水在调节热稳定性蛋白质中的关键作用。
DOI：
10.1021/jp805199c
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发表时间：
2009
期刊：
影响因子：
--
通讯作者：
S. Melchionna
中科院分区：
文献类型：
--
作者：
Fabio Sterpone;C. Bertonati;G. Briganti;S. Melchionna
通过分子动力学模拟研究了3种具有嗜温、嗜热和超嗜热特征的同源蛋白质在4种不同温度下的热稳定性，以探讨水对热稳定性的控制作用。暴露于水的蛋白质的表面示出增加的嗜热性的程度，和水在提高蛋白质内部的灵活性和结构的鲁棒性的作用得到阐明。包封的大分子的水-水氢键簇的存在下，示出与热鲁棒性时，从嗜中温到超嗜热的变体。我们的分析表明，热稳定性的重要贡献源于蛋白质-水表面效应，而蛋白质的内部包装起着次要的作用。
Three homologous proteins with mesophilic, thermophilic and hyperthermophilic character have been studied via molecular dynamics simulations at four different temperatures in order to investigate how water controls thermostability. The water-exposed surface of the protein is shown to increase with the degree of thermophilicity, and the role of water in enhancing the protein internal flexibility and structural robustness is elucidated. The presence of water-water hydrogen bond clusters enveloping the macromolecule is shown to correlate with thermal robustness when going from the mesophilic to the hyperthermophilic variants. Our analysis indicates that essential contributions to thermostability stem from protein-water surface effects whereas the protein internal packing plays a minor role.