We apply EPR methods like DEER to probe distances between two spin labels introduced in biomolecules. As a recent development, the use of Gd3+ as a paramagnetic center rather than nitroxides opens new opportunities with respect to their stability and magnetic properties.
Being able to determine the structure of proteins, on the atomic level, in their native environment, the cell, and follow structural transformation they undergo in the cell upon interaction with other cellular components is of major importance for understanding their function.
Our microfluidic rapid freeze-quench design allows us to trap and investigate changes of protein conformation and structure in a time-resolved manner. The improves design is optimized for very small sample volumes, allowing the investigation of proteins that are difficult to obtain.
In our group, we employ two home-built spectrometers, which are subject to continuous improvement. Additionaly, our research is focused towards the development and improvement of novel experiments, leading to increased sensitivity and applicability.
Nuclear Magnetic Resonance (NMR) is witnessing a revolution, being driven by the advent of new methods with high potential for achieving nuclear hyperpolarization. It has been recently demonstrated that new technologies based on dynamic nuclear polarization (DNP), whereby the large spin alignment characteristic of electron paramagnetic resonance is passed on to nuclear spins at low temperatures, can be used to increase the sensitivity of typical NMR and MRI experiments by >10,000 times.