We are interested in the structural enzymology of proteins responsible for blood coagulation, with the goal of unraveling the molecular architecture and mechanism of the underlying interactions. Our approach uses a combination of conventional (rapid kinetics, protein engineering, X-ray crystallography) and innovative (smFRET, cryo-EM) biophysical techniques.

We currently focus on the interaction of prothrombin with prothrombinase, leading to generation of thrombin and blood clotting, the activation of factor V required for assembly of prothrombinase and the interaction of the thrombin-thrombomodulin complex with protein C that halts the coagulation response. Current studies also focus on factor V short and its interactions with TFPIalpha, protein S and factor Xa. Emerging interests include proteins of the contact pathway like factors IX, XI and XII.