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理解和应用疏水相互作用的尺度依赖原理
引用本文:邸维帅,王娟,梅岳海,曹毅.理解和应用疏水相互作用的尺度依赖原理[J].物理学进展,2020,40(1):1-18.
作者姓名:邸维帅  王娟  梅岳海  曹毅
作者单位:南京大学物理学院固体微结构物理国家重点实验室;南京大学脑科学研究院;南京大学智能光学传感与集成重点实验室
摘    要:Lum,Chandler 和Week 三人建立起来的尺度依赖的疏水相互作用理论为人们提供了一个 重要的理论框架(LCW 理论)去理解和进一步研究与疏水相互作用相关的现象。按照LCW 理 论,当一个疏水粒子的半径小于1 纳米,它的疏水水合自由能与其半径的三次方成线性关系;而当 一个疏水粒子的半径大于1 纳米,它的疏水水合自由能与其半径的二次方成线性关系。1 纳米是一 个较为普适的转变半径。小于这个尺度,水合的热力学过程是由熵主导的,大于这个尺度,水合的 热力学过程是由焓主导的。在这篇综述里,我们介绍了温度,压强和水里面的添加物对疏水水合自 由能的影响。在实验上,我们对基于原子力显微镜的单分子力谱方法研究疏水高分子水合能作了重 点介绍。同时,对这一理论在蛋白质折叠和膜组装等体系中的应用也做了介绍。

关 键 词:疏水相互作用    尺度依赖原理    单分子力谱    疏水驱动力    蛋白质折叠    膜组装

Understanding and Applying the Length-scale Dependence Mechanism of Hydrophobic Interaction
Di Wei-Shuai,Wang Juany,Mei Yue-Hai,Cao Yi.Understanding and Applying the Length-scale Dependence Mechanism of Hydrophobic Interaction[J].Progress In Physics,2020,40(1):1-18.
Authors:Di Wei-Shuai  Wang Juany  Mei Yue-Hai  Cao Yi
Institution:(Collaborative Innovation Center of Advanced Microstructures,National Laboratory of Solid State Microstructure,Department of Physics,Nanjing University,Nanjing 210093,China;Institute for Brain Sciences,Nanjing University,Nanjing 210023,China;Key Laboratory of Intelligent Optical Sensing and Integration,Nanjing University,Nanjing 210023,China)
Abstract:The length-scale dependence theory established by Lum,Chandler and Week provided a new insight into interpreting,studying and applying hydrophobic interaction.Hydrophobic hydration free energy decreases with the volume of solute at small length regime(<1 nm)and increases with the surface area of solute at a larger length regime(>1 nm).The crossover length near 1 nm indicates an entropic and enthalpic co-dominant hydration process at micro level which is distinct to the macro-level phenomenon.In this review,we showed the dependence of hydrophobic hydration free energy on temperature,pressure and additives.Especially,single-molecule force spectroscopy was introduced to provide a method to investigate hydrophobic interaction with respect to polymers.Furthermore,various applications relevant to hydrophobic interaction were represented to inspire deeper researches and explorations.Moreover,hydrophobic interaction underlying the protein folding and membrane assembly was further understood based on these promising progresses.
Keywords:Hydrophobic Interaction  Length-scale Dependence  Single-Molecule Force Spectroscopy  Driving Force  Protein Folding  Membrane Assembly
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