Even though my main expertise is focused on the simulations of dynamics-driven processes of biomolecules, I am pursuing a research line that is made of both experiments and computations, as the combination of these two approaches is extremely powerful to outline the behavior of molecules.
You will find a fair share of my work characterized by the presence of both experiments and simulations. I am a strong advocate of integrated and multidisciplinary research because molecular processes, even at a single molecule level, are extremely complex and only the combination of multiple techniques can provide an exhaustive understanding of the different facets characterizing their behavior.
Especially regarding the combination of experiments and simulations, the two fields can really benefit from each other. Simulations can use experimental observables to sample meaningfully the behavior of molecular structure and dynamics, while simulations can provide both a range of predictions for the development of new hypothesis and, more importantly, an atomic resolved picture of the investigated system. In the past few years we have seen an increasing number of studies that combine the two and I believe that this trend will only get stronger.
Using cross-collaborative approaches I have investigated several processes of biological interest: from the binding of enzymes to their substrates, to the study of binding and dynamics of intrinsically disordered proteins.
During my PhD I have carried out investigations of protein-protein and protein-carbohydrate interactions as, for example, the binding and mechanism of action of proteins called pectin-methylesterases. These enzyme have the particularity to act as molecular motors on linear polysaccharides without the employment of additional energetic co-factors. This makes them especially interesting for industrial applications. More recently, during my 4-years postdoctoral experience as a computational biophysicist at The Heidelberg Institute for Theoretical Studies & Heidelberg University, I have been involved in the study of Intrinsically Disordered Proteins (IDPs). In particular, I have tackled the problem of reproducing their correct dynamics using molecular dynamics simulations because force fields, mostly developed and optimized over decades for structured proteins, fail at reproducing the correct ensemble dimensions of IDPs and artificially tend to collapse them.
I have then also investigated the binding of nucleoporins to nuclear transport receptors, discovering an interesting new mechanism of binding that doesn’t follow the more commonly described induced fit or conformational selection. The results of these investigations have been recently published and you can look up for more details into my publications page.
Beyond these, I am following a series of other projects that you can overview in my current projects page. Hope that you will find them interesting!