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

Magnetic Resonance Letters 2026 Open access

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Authors: Thomas W. Redvanly, Gary J. Pielak
DOI: 10.1016/j.mrl.2026.200305
Cited by: 1
References: 22

Abstract

F 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.

Fields of Study & Subjects

thermodynamics and calorimetric analyses Protein Structure and Dynamics Hemoglobin structure and function

Publication details

Journal / source
Magnetic Resonance Letters
Publisher
Elsevier BV
Volume
7
Issue
1
Pages
200305–200305
Publication date
4 August 2026
Language
EN