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Updated: Aug 24, 2026

Disentangling Glycan-Protein Interactions: Nuclear Magnetic Resonance (NMR) to the Rescue
Published on: May 17, 2024
Using 19F NMR to quantify enthalpy-entropy compensation in protein-protein interactions
Thomas W Redvanly1, Gary J Pielak1,2,3,4
1Department of Chemistry, University of North Carolina at Chapel Hill (UNC-CH), Chapel Hill, NC, USA, 27599-3290.
None:
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.
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