A considerable number of cellular machineries depend on highly specific interactions between protein, RNA or DNA receptors and their small-molecule ligands, such as cofactors, hormones, drugs or metabolites. Knowledge of the interactions involved is critical for understanding bimolecular recognition implicated in signaling and for developing new therapeutic solutions. The complete comprehension of the intermolecular interactions requires a full characterization of the geometry and the dynamics of the complex.
Moreover the description of the intermolecular dynamics is known to be critical information but it is still not available due to lack of technique. A 3D structure of a molecule with its dynamics is certainly the most quantitative information in molecular sciences but we still use it semi-qualitatively or qualitatively. There is the need to apply structural biophysics methods as a quantitative tool in molecular pharmacy.
Therefore we investigate structure, function and dynamics of protein-ligand complexes. We try to identifying small-molecule inhibitors of functionally relevant macromolecular interactions. To achieve that goals we developed multidisciplinary approaches combining NMR spectroscopy, X-ray crystallography and computational methods.