Related Experiment Video
Updated: May 8, 2026

Unraveling Entropic Rate Acceleration Induced by Solvent Dynamics in Membrane Enzymes
Published on: January 16, 2016
Entropy-enthalpy Compensation of Biomolecular Systems in Aqueous Phase: a Dry Perspective
Liviu Movileanu1, Eric A Schiff
1Department of Physics, Syracuse University, Syracuse, New York USA.
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.
Related Concept Videos
Enthalpy of Solution
Entropy and Solvation
Enthalpy within the Cell
H = U + PV
Enthalpy is also a state function. Enthalpy values for specific substances cannot be measured directly; only enthalpy changes for chemical or physical processes can be determined. For processes that take place at constant pressure (a common condition for many chemical...
Entropy Changes Accompanying Specific Processes
Standard Entropy Change for a Reaction
Enthalpy

