Entropy Changes in Water Networks Promote Protein Denaturation.

Yichong Wang, Junlang Liu, Michael M Peters, Ryoma Ishii, Dianzhuo Wang, Sourav Chowdhury, Kevin Kit Parker, Eugene I Shakhnovich
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Abstract

For over a century, an explanation for how concentrated ions denature proteins has proven elusive. Here, we report a novel mechanism of protein denaturation driven by entropy changes in water networks. Experiments and simulations show that ion pairs like LiBr and LiCl localize water molecules and disrupt the water network's structure, while others exert a more global effect without compromising network integrity. This disruption reduces the entropy penalty when proteins sequester water molecules during unfolding, resulting in a peculiar yet universal "inverse hydrophobic effect" that potentiates protein denaturation. Through successful isolation and systematic study of indirect solute effects, our findings offer a universal approach to salt induced protein denaturation and provide a unified framework for the decoding of the protein-water-solute nexus.

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熵驱动变性,实现蛋白质废弃物的可持续再生。
电解质是所有生命形式环境的重要组成部分,蛋白质、水和溶质在其中相互作用,支持生命活动。然而,一个多世纪以来,人们一直未能从根本上了解离子溶质对蛋白质的影响。在这里,我们展示了一些离子溶质是如何在蛋白质与离子之间没有直接相互作用的情况下充当强效变性剂的。我们展示了不同离子溶质变性效力之间的巨大差异,其中溴化锂(LiBr)是最强的变性剂,而溴化钠(NaBr)的变性效力最低。实验和模拟表明,某些离子的存在会破坏水网络结构,从而通过熵驱动机制间接诱导蛋白质变性。通过对间接溶质效应的成功分离和系统研究,我们的发现为蛋白质-水-溶质关系的解码提供了一个统一且普遍适用的框架,所有当前的研究都可以很容易地纳入其中。此外,我们的再生方法强调了以可持续的方式将蛋白质废物重新利用为有价值的生物材料的可行性,具有广泛的应用潜力。
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