Predicting the binding free energy of proteins provides new opportunities to modulate and control protein-protein interactions. However, existent methods rely on the structure of the complexes to make predictions, seriously limiting the applicability to few interactions.

The BADock server implements a novel strategy that use the non-specific complexes obtained by docking to predict the free energy, allowing the user to predict the binding affinities from the unbound tertiary structures. We have tested the approach on a set of globular and soluble proteins of the newest affinity benchmark, obtaining a prediction accuracy comparable to other state-of-art methods.

Input file(s)

Files must be protein structures in PDB format: .pdb extension.