The research projects in my group are focused on the study of protein folding, design and evolution using solution Nuclear Magnetic Resonance spectroscopy and a variety of complementary biophysical methods. How does a protein fold into it specific tridimensional structure and evolve to perform a given biological function remain key questions in most modern day diseases. Especially when combined with high-pressure perturbation, NMR spectroscopy offers the opportunity to characterize protein free-energy landscapes at an atomic resolution.

Related projects include the study of intrinsically disordered proteins, the characterization of amyloid-type peptides and the development of coarse-grained methods for protein folding simulations.