Journal of the American Chemical Society · 1996 · 184 citations · 19 references
Natural SciencesBiophysicsPhysicsMolecular PhysicsPhysical ChemistryThermodynamicsChemical ThermodynamicsEntropyFree EnergyHydrationSolvation ModelingSolvation TheoryEnthalpyEnthalpy ChangeFinite Mixture ModelsHydration BehaviorHydration EnthalpyHydration EntropyHydration Free EnergyHydrophobic Bonding
Hydrophobic hydration models attribute the large free‑energy change to hydrogen‑bond rearrangements, yet these models conflict with the observation that enthalpy and entropy largely compensate, as illustrated by Muller's two‑state model which yields small enthalpy and large negative entropy. The study investigates Muller's two‑state model to determine whether it can generate nearly compensating enthalpy and entropy changes. The authors find that minimal modifications to Muller's model suffice to produce nearly compensating enthalpy and entropy changes.
Many of the mixture models of water seek to explain the large free energy change associated with hydrophobic hydration by means of changes in the number and character of the hydrogen bonds in water. All of these models, regardless of detail, are in clash with the idea that hydrogen bond rearrangements will produce changes in both enthalpy and entropy, which largely compensate to produce little net free energy change. One of the simplest and most recent of these mixture models is Muller's two-state model, which produces small enthalpy and large negative entropy changes. In this paper, Muller's model is examined in detail. It is found that only slight changes are required in order for the model to produce nearly compensating enthalpy and entropy changes.
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The Hydrophobic Effect: Formation of Micelles and Biological Membranes
C.H. Walker · FEBS Letters · 1981 · 2.7K citations