Direct measurement of protein binding energetics by isothermal titration calorimetry.

By Stephanie A. Leavitt, E. Freire. Current Opinion in Structural Biology, 2001

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Interactions between Polyphenols and Macromolecules: Quantification Methods and Mechanisms (2012, background): “The free energy (ΔG) and entropy (ΔS) of binding are determined from the association constant [ Wiseman et al, 1989 ; Leavitt & Freire, 2001 ].”
Interactions between milk proteins and polyphenols: Binding mechanisms, related changes, and the future trends in the dairy industry (2018, background): “Soares et al.[61] reported that presence of a galloyl group on catechins enhances the binding affinity to BSA and similar results were observed by Skrt et al.[62] Bohin et al.[48] was not able to find a measurable interaction between BSA and catechin or epicatechin whereas an extra galloyl group on ”
Thermodynamic consequences of disrupting a water‐mediated hydrogen bond network in a protein:pheromone complex (2005, methodology): “Furthermore, the binding enthalpy calculated from the MUP-I:SBT structure using the semiempirical approach of Freire and coworkers (Leavitt and Freire 2001; VelazquezCampoy et al. 2001) is close to the observed value only when the buried water molecules are accounted for in the calculation, suggesti”
Predicting the Effect of Mutations on Protein-Protein Binding Interactions through Structure-Based Interface Profiles (2015, background): “Quantitatively, ΔΔG values for protein interactions may be measured experimentally by a variety of biophysical techniques [4, 5].”