Using ¹⁹F NMR to quantify enthalpy-entropy compensation in protein-protein interactions.

Authors

Thomas W Redvanly, Gary J Pielak

Published in

Magnetic resonance letters. Volume 7. Issue 1. Pages 200305. Epub Aug 04, 2026.

Abstract

Protein structural, stability, and functional equilibria are sensitive to the solution environment and governed by enthalpic and entropic contributions. NMR spectroscopy of suitably labeled- or isotopically enriched-samples provides a powerful tool for quantifying protein reactions in solution. Here we apply ¹⁹F NMR data, acquired in a systematic effort to assess the equilibrium crowding effects of polyethylene glycols (PEGs), to reveal the first quantitative evidence for enthalpy-entropy compensation in protein-protein complexes. Analysis of the effects of PEG molecular weight and concentration reveals that changes in polymer -mesh size and -concentration produce proportional, compensatory shifts in the enthalpic and entropic components of dimer dissociation.

PMID:
42633206
Bibliographic data and abstract were imported from PubMed on 23 Aug 2026.

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