dorsal/arxiv
View SchemaScaled-Particle Theory and the Length-scales Involved in Hydrophobic Hydration of Aqueous Biomolecular Assemblies
| Authors | Henry S. Ashbaugh, Lawrence R. Pratt |
|---|---|
| Categories | |
| ArXiv ID | physics/0307109 |
| URL | https://arxiv.org/abs/physics/0307109 |
Abstract
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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"abstract": "Hydrophobic hydration plays a crucial role in self-assembly processes over\nmultiple length-scales, but the extrapolation of molecular-scale models to\nlarger length-scale hydration phenomena is sometimes not warranted.\nScaled-particle theories are based upon an interpolative view of that issue. We\nrevisit the scaled-particle theory proposed thirty years ago by Stillinger,\nadopt a practical generalization, and consider the implications for hydrophobic\nhydration in light of our current understanding. The generalization is based\nupon identifying a molecular length, implicit in previous applications of\nscaled-particle models, that provides an effective radius for joining\nmicroscopic and macroscopic descriptions. We demonstrate that the generalized\ntheory correctly reproduces many of the anomalous thermodynamic properties of\nhydrophobic hydration for molecularly sized solutes, including solubility\nminima and entropy convergence, successfully interpolates between the\nmicroscopic and macroscopic extremes, and provides new insights into the\nunderlying molecular mechanisms. The results are discussed in terms of\nlength-scales associated with component phenomena; in particular we first\ndiscuss the micro-macroscopic joining radius identified by the theory, then we\ndiscuss in turn the Tolman length that leads to an analogous length describing\ncurvature corrections of a surface area model of hydrophobic hydration free\nenergies, and the length-scales on which entropy convergence of hydration free\nenergies are expected.",
"arxiv_id": "physics/0307109",
"authors": [
"Henry S. Ashbaugh",
"Lawrence R. Pratt"
],
"categories": [
"physics.bio-ph",
"physics.chem-ph"
],
"title": "Scaled-Particle Theory and the Length-scales Involved in Hydrophobic Hydration of Aqueous Biomolecular Assemblies",
"url": "https://arxiv.org/abs/physics/0307109"
},
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