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首页> 外文期刊>Physical chemistry chemical physics: PCCP >Comment on 'Thermal compaction of the intrinsically disordered protein tau: entropic, structural, and hydrophobic factors'' by A. Battisti, G. Ciasca, A. Grottesi and A. Tenenbaum, Phys. Chem. Chem. Phys., 2017, 19, 8435
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Comment on 'Thermal compaction of the intrinsically disordered protein tau: entropic, structural, and hydrophobic factors'' by A. Battisti, G. Ciasca, A. Grottesi and A. Tenenbaum, Phys. Chem. Chem. Phys., 2017, 19, 8435

机译:评论“本质上紊乱的蛋白质TAU的热压实:A.Battisti,G. Ciacha,A. Grottesi和A. Tenenbaum,Phys。化学。Chem.Chem.Chem.Chem.Chem.Chem。,物理。,2017,19 ,8435

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In a recent article, A. Battisti et al., Phys. Chem. Chem. Phys., 2017, 19, 8435, results from SAXS measurements, metadynamic trajectories and classic MD trajectories at different temperatures have been used to study the temperature-induced compaction of the intrinsically disordered protein tau. The analysis, though technically sound, does not provide a clear explanation of hydrophobic interaction strengthening on increasing the temperature and its relationship with the population increase of secondary structural elements. Actually, hydrophobic interaction is driven by the gain in translational entropy of water molecules associated with the decrease in solvent-excluded volume due to chain compaction. The magnitude of this solvent-excluded volume effect increases with temperature in water because the density of water is almost temperature-independent due to the strength of H-bonds. Since a-helix formation leads to a significant decrease in the solvent-excluded volume, the connection with hydrophobic interaction and chain compaction emerges directly.
机译:在最近的一篇文章中,A. Battisti等,Phy。化学。化学。 Phys,2017,19,8435,SAXS测量结果,不同温度的MetadnyciC轨迹和经典MD轨迹的结果已经用于研究本质无序蛋白Tau的温度诱导的压实。虽然技术上,分析不提供关于增加温度的疏水相互作用和其与次级结构元素的群体增加的关系的明确解释。实际上,疏水相互作用由与链压缩引起的溶剂排除量减少相关的水分子的平移熵的增益驱动。这种溶剂排除体积效果的幅度随着水中的温度而增加,因为由于H键的强度,水的密度几乎是温度无关的。由于A-Helix形成导致溶剂排除体积的显着降低,因此与疏水相互作用和链压的连接直接出现。

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