Magnetic resonance spectroscopy is a powerful method to obtain atomic-level structural information on complex molecular systems. Nuclear magnetic resonance (NMR) spectroscopy probes the nuclei, while its magnetic resonance sister technique, electron paramagnetic resonance (EPR) spectroscopy, probes the unpaired electrons. In our group we use both forms of magnetic resonance spectroscopy to study the structure, function, and operating mechanisms of biological macromolecules.

An important part of our work is the advancement of NMR and EPR methodology. In physical chemistry, "finding new ways to measure things" goes hand in hand with application. A biological question is an incentive to develop a method. The new method gives new information about the biological system. As we learn more, new questions come up, which ask for new methods, and so on. This makes the research in our group very interdisciplinary and we often encounter physics, chemistry, biology, and engineering within the same day.

Continue reading about our research here.

Our research is funded by the Deutsche Forschungsgemeinschaft (DFG) through the Emmy Noether program.