Dörte Rother
Selin Kara
Jan von Langermann
Jennifer Littlechild
Uwe Bornscheuer
Helen Hailes
Helen received her Ph.D in 1991 at Cambridge under the supervision of Professor Jim Staunton. She pursued post-doctoral work at Cambridge, and then at Imperial College London with Professor Steve Ley and subsequently with Dr David Widdowson. She joined the Department of Chemistry, University College London as a Lecturer in 1994, becoming a Senior Lecturer in 2002, a Reader in 2005, and Professor of Chemical Biology in 2010.
Research is focused on the development of new sustainable chemistry approaches for use in synthesis. Several projects involve the discovery, optimisation and use of biocatalysts in single or multi-step pathways to construct single isomer biologically active molecules. In addition, we are investigating reactions and multi-step synthetic biology cascades in water and other green solvents.
Bernhard Hauer
Reinhard Sterner
Reinhard Sterner studied Biology (Diploma) at the University of Munich (Germany) from where he graduated in 1988. He performed his doctoral studies at the same university and obtained a PhD in 1991 under the supervision of Prof. Heinz Decker. He then moved on to the Biocentre of the University of Basel (Switzerland) where he worked as a postdoctoral fellow with Prof. Kasper Kirschner and completed his Habilitation in Biochemistry in 1996. Reinhard Sterner was then awarded a Heisenberg fellowship from the German Research foundation (DFG), which enabled him in 1997 to set up a junior research group at the University of Göttingen (Germany). In 1999, he was appointed associate professor of Biochemistry at the University of Cologne (Germany). In 2004, he relocated to the University of Regensburg (Germany) where he has been working since then as a full professor of Biochemistry. The main research interests of Prof. Sterner are enzyme engineering, enzyme evolution, and the structure-function relationship of multi-enzyme complexes.
"The engineering of existing enzymes and the design of novel enzymes with a preconceived combination of stability and activity is a highly ambitious and relevant goal of protein biochemistry. Our ability to generate such tailored enzymes would have great implications for our understanding of the structure-function relationship of proteins and holds promise for many medical and biotechnological applications."
Donald Hilvert
