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An information theory model is used to construct a molecular explanation whyhydrophobic solvation entropies measured in calorimetry of protein unfoldingconverge at a common temperature. The entropy convergence follows from the weaktemperature dependence of occupancy fluctuations for molecular-scale volumes inwater. The macroscopic expression of the contrasting entropic behavior betweenwater and common organic solvents is the relative temperature insensitivity ofthe water isothermal compressibility. The information theory model provides aquantitative description of small molecule hydration and predicts a negativeentropy at convergence. Interpretations of entropic contributions to proteinfolding should account for this result.Comment: Phys. Rev. Letts. (in press 1996), 3 pages, 3 figure

Origin of Entropy Convergence in Hydrophobic Hydration and Protein Folding