Tilman Schirmer is interested in molecular mechanisms of bacterial signal transduction. He is a trained Crystallographer, but has extended his activities into functional characterization and kinetic modeling to reveal structure - function relationships. He has graduated at the Max-Planck Institute in Martinsried (Germany) and has worked at the LMB Cambridge (UK) on the regulation of phosphofructokinase. He then moved to the Biozentrum Basel (Switzerland) to reveal the structure and translocation mechanism of maltoporin. His current interest lies mainly in the various aspects of c-di-GMP signaling and FIC-mediated AMPylation of target proteins. Tilman Schirmer is interested in molecular mechanisms of bacterial signal transduction. He is a trained Crystallographer, but has extended his activities into functional characterization and kinetic modeling to reveal structure - function relationships. He has graduated at the Max-Planck Institute in Martinsried (Germany) and has worked at the LMB Cambridge (UK) on the regulation of phosphofructokinase. He then moved to the Biozentrum Basel (Switzerland) to reveal the structure and translocation mechanism of maltoporin. His current interest lies mainly in the various aspects of c-di-GMP signaling and FIC-mediated AMPylation of target proteins.

Structural Biology