The research activity of the group is focused on the computational study of protein dynamics and its relationship to protein function.
The main interest of the group is the study of structural, dynamical and mechanical properties of proteins from the cardiac muscle. Heart contraction arises from a complex interplay of precisely timed molecular motions and the identification of new therapeutic targets for cardiomyopathies relies on a deep understanding of these mechanisms. Combining Molecular Modelling, Molecular Dynamics simulation and Bioinformatics techniques, we investigate how post-translational modifications and cardiomyopathy-related mutations affect the protein motion and stability.
The group is also involved in the development of computational methods for the study of conformational transitions in proteins. In addition to promoting the motion of molecular motors, conformational changes can be essential for many protein functions and they are often required for protein-protein interaction and allosteric regulation. The group aims at improving both the sampling and the detection of biologically relevant conformational transitions, which are usually beyond the timescale of traditional molecular simulations.