We study proteins' conformational changes and dynamic interplay of biomacromolecules in model membranes and in organelles by means of site-directed spin labeling electron paramagnetic resonance (EPR). This technique bridges the gap between static protein snapshots, which can be provided by crystallographic methods, and dynamic conformational transitions of proteins during their function. We use Double Electron-Electron Resonance (DEER) to extract interspin distances on spin-labeled membrane proteins. Conventional nitroxide-based as well as newly developed orthogonal labeling strategies are used, to selectively pinpoint specific distances in protein networks under physiological conditions.

• ABC transporters: mechanism of action of heterodimeric exporters

• Mapping the interaction network and the conformational changes of Bcl-2 proteins during cell death