  An information theory model is used to construct a molecular explanation why
hydrophobic solvation entropies measured in calorimetry of protein unfolding
converge at a common temperature. The entropy convergence follows from the weak
temperature dependence of occupancy fluctuations for molecular-scale volumes in
water. The macroscopic expression of the contrasting entropic behavior between
water and common organic solvents is the relative temperature insensitivity of
the water isothermal compressibility. The information theory model provides a
quantitative description of small molecule hydration and predicts a negative
entropy at convergence. Interpretations of entropic contributions to protein
folding should account for this result.
