An Analysis of the Thermodynamics of Hydrophobic Solvation Based on Scaled Particle Theory

2001/04/25 by Hong Qian, Qian, Hong
Engineering · #Biological Physics (physics.bio-ph) #Biomolecules (q-bio.BM) #FOS: Biological sciences #FOS: Physical sciences #Lattice Boltzmann Simulation Studies

paper · pdf · doi:10.48550/arxiv.physics/0104085

openalex publication_date 2001/04/25 · openalex created_date 2025/10/10 · openalex updated_date 2026/07/28

Abstract

A comprehensive, semi-quantitative model for the thermodynamics of hydrophobic solvation is presented. The model is based on a very simple premise suggested by the scaled particle theory and treats both solute and solvent molecules as hard spheres. A connection between the peculiarly large heat-capacity change for hydrophobic solvation and the large temperature dependence of the thermal expansivity of water is found. Analysis reveals a possible physical origin for the converging behavior of solvation entropies for a series of homologous hydrophobic compounds. The model suggests that the low solubility and the large heat-capacity change of hydrophobic solvation stem from two distinct aspects of water molecules: the static geometry of the molecule and the dynamic hydrogen bonding network, respectively.

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