Entropy-enthalpy compensation of biomolecular systems in aqueous phase: A dry perspective

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17 Scopus citations


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.

Original languageEnglish (US)
Pages (from-to)59-65
Number of pages7
JournalMonatshefte fur Chemie
Issue number1
StatePublished - Jan 2013


  • Biological macromolecules
  • Entropy-enthalpy compensation
  • Hydrophobic interactions
  • Macromolecules

ASJC Scopus subject areas

  • General Chemistry


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