We have conducted computational and experimental studies of the membrane binding of some peripheral membrane binders. In particular, we have earned insights into the binding of serine protease 3 (PR3) and a bacterial Phospholipase C.
We develop and apply computational methods for the characterisation and comparison of the collective motions of protein structures mostly through the use of elastic network models and normal mode analysis. We implemented and maintain the WEBnm@ server which offers many useful analyses of normal modes, and also allows for comparative analyses of aligned proteins through a user-friendly interface.
During the last 10 years, we have uncovered key features on ligand recognition and structure-activity relationships of specific regulators of inflammation. The early work in the group has paved our current activity which focuses on the development of inhibitors with a diagnostic or therapeutic potential in chronic inflammatory diseases.
Despite knowing so much more about enzymes than we ever have before, we realise that we have only scratched the surface of what can be known about them. The challenges with “Enzyme discovery” are manifold; we focus on defining enzyme families based specific characteristics and annotating large environmental samples with unknown extremophiles in order to find novel enzymes.