Origin of entropy convergence in hydrophobic hydration and protein folding
Origin of entropy convergence in hydrophobic hydration and protein folding
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DOI：
10.1103/physrevlett.77.4966
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发表时间：
1996-12-09
影响因子：
8.6
通讯作者：
Pratt, LR
中科院分区：
文献类型：
--
作者：
Garde, S;Hummer, G;Pratt, LR
利用信息论模型对蛋白质去折叠量热法测量的疏水溶剂化熵在同一温度下收敛的原因进行了分子解释。熵收敛来自于水分子尺度体积的占位起伏对温度的弱依赖性。水与一般有机溶剂熵行为的对比，宏观上表现为水的等温压缩性对温度的相对不敏感性。信息论模型提供了一个定量的描述小分子水化，并预测收敛时的负熵。熵对蛋白质折叠的贡献的解释应该解释这个结果。
An information theory model is used to construct a molecular explanation why hydrophobic solvation entropies measured in calorimetry of protein unfolding converge at a common temperature. The entropy convergence follows from the weak temperature dependence of occupancy fluctuations for molecular-scale volumes in water. The macroscopic expression of the contrasting entropic behavior between water and common organic solvents is the relative temperature insensitivity of the water isothermal compressibility. The information theory model provides a quantitative description of small molecule hydration and predicts a negative entropy at convergence. Interpretations of entropic contributions to protein folding should account for this result.