Scaled-Particle Theory and the Length-scales Involved in Hydrophobic Hydration of Aqueous Biomolecular Assemblies

Details Scaled-Particle Theory and the Length-scales Involved in Hydrophobic Hydration of Aqueous Biomolecular Assemblies Scaled-Particle Theory and the Length-scales Involved in Hydrophobic Hydration of Aqueous Biomolecular Assemblies

2003-07-22

arxiv.org/abs/physics/0307109v2

Physics

Biological Physics

19 pages, 14 figures, one figure added, submitted to Rev. Mod. Phys

Scientific paper

Hydrophobic hydration plays a crucial role in self-assembly processes over multiple length-scales, but the extrapolation of molecular-scale models to larger length-scale hydration phenomena is sometimes not warranted. Scaled-particle theories are based upon an interpolative view of that issue. We revisit the scaled-particle theory proposed thirty years ago by Stillinger, adopt a practical generalization, and consider the implications for hydrophobic hydration in light of our current understanding. The generalization is based upon identifying a molecular length, implicit in previous applications of scaled-particle models, that provides an effective radius for joining microscopic and macroscopic descriptions. We demonstrate that the generalized theory correctly reproduces many of the anomalous thermodynamic properties of hydrophobic hydration for molecularly sized solutes, including solubility minima and entropy convergence, successfully interpolates between the microscopic and macroscopic extremes, and provides new insights into the underlying molecular mechanisms. The results are discussed in terms of length-scales associated with component phenomena; in particular we first discuss the micro-macroscopic joining radius identified by the theory, then we discuss in turn the Tolman length that leads to an analogous length describing curvature corrections of a surface area model of hydrophobic hydration free energies, and the length-scales on which entropy convergence of hydration free energies are expected.

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