Origin of Heat Capacity Changes in a “Nonclassical” Hydrophobic Interaction

Ebb and flow. We examined the negative change in heat capacity (ΔCp) in a hydrophobic interaction (recombinant mouse major urinary protein–hydrophobic ligand) with a “nonclassical” enthalpy-driven binding signature and found that the change in heat capacity was almost entirely dominated by desolvation of the ligand. We conclude that the thermodynamic signatures of the “classical” and “nonclassical” hydrophobic effect are both dominated by solvent reorganization.