Intermolecular Contact Potentials for Protein-Protein Interactions Extracted from Binding Free Energy Changes upon Mutation.

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Predicting the Effect of Mutations on Protein-Protein Binding Interactions through Structure-Based Interface Profiles (2015, methodology): “The residue level contact potential of Moal and Fernandez-Recio [14] achieves a similar performance of c = 0.”
SKEMPI 2.0: an updated benchmark of changes in protein–protein binding energy, kinetics and thermodynamics upon mutation (2018, methodology): “The first release has been used as a basis for many further studies, including the development of energy functions (Moal and Fernandez-Recio, 2013; Moal et al., 2015b) which were subsequently implemented in the CCharPPI web server for characterizing protein–protein interactions (Moal et al.”
The scoring of poses in protein-protein docking: current capabilities and future directions (2013, methodology): “AP_DDGru [76] r The unweighted intermolecular contact potential extracted from ΔΔG data.”