title: Entropy-enthalpy Compensation of Biomolecular Systems in Aqueous Phase: a Dry Perspective.
abstract: We survey thermodynamic measurements on processes involving biological macromolecules in aqueous solution, which illustrate well the ubiquitous phenomenon of entropy-enthalpy compensation. The processes include protein folding/unfolding and ligand binding/unbinding, with compensation temperatures varying by about 50 K around an average near 293 K. We show that incorporating both near-exact entropy-enthalpy compensation (due to solvent relaxation) and multi-excitation entropy (from vibrational quanta) leads to a compensation temperature in water of about 230 K. We illustrate a general procedure for subtracting solvent and environment-related terms to determine the bare Gibbs free energy changes of chemical processes.
authors: Department of Physics, Syracuse University, Syracuse, New York USA.
authors: Liviu
authors: L
authors: Movileanu
authors: Eric A
authors: EA
authors: Schiff
keywords: Biological macromolecules; Entropy-enthalpy compensation; Hydrophobic interactions; Macromolecules
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