Prof. Dr. Stephan Grzesiek

University of Basel
Klingelbergstrasse 50 / 70
CH - 4056 Basel
Biozentrum, Room 386 Phone: +41 61 207 21 00
Curriculum Vitae

Administrative Assistant

Jacqueline Staub
Biozentrum, Room 308
Phone: +41 61 207 21 01
Fax: +41 61 207 21 09


New insights into the function of the main class of drug targets

About thirty percent of all medical drugs such as beta-blockers or...more

New insights into survival strategies of bacteria

Even the simplest cells such as bacteria have developed effective strategies to...more

Interaction between two leukemia drugs explained

Currently no treatment option is available for five percent of patients...more

Research group Stephan Grzesiek

Understanding biomolecular function

Nuclear magnetic resonance methods provide unique insights into the structure, dynamics, and interactions of biomolecules.

NMR spectroscopy reveals atomic details of drug-induced signaling in the β1-adrenergic G-protein coupled receptor.

All biological processes, for example cell division, infection or development of cancer, are based on specific interactions between biomolecules. These interactions are consequences of the atomic structures of biomolecules and their changes with time. Nuclear magnetic resonance (NMR) can determine both structure and dynamics of biomolecules and their complexes in solution. This makes it possible to understand biomolecular function at a fundamental level and also to develop strategies for interfering with function, e.g. by drugs.

Disease-relevant proteins

Our research is focused on problems in structural biology where NMR can yield unique new information on biomolecular structure, dynamics, and function. In particular, we are interested in molecules associated with human diseases, such as Abl kinase, a protein responsible for the development of chronic myeloid leukemia, the HIV-1 coreceptor CCR5, the β1-adrenergic receptor, or lipopolysaccharide, the molecule responsible for endotoxic shock.

Further development of NMR methods

A second focus is the development of new NMR methods that yield a better description of protein structure, dynamics and physicochemical interactions. In particular, we are developing new technologies for a highly quantitative description of unfolded protein states and of hydrogen bonds.