Our research is centered on the development of new tools in solid state NMR to determine the 3D structures of insoluble proteins such as fibrils and other supramolecular assemblies, as well as membrane proteins. Common to the proteins we work on is that they remain inaccessible to other structural methods. The biological systems include proteins involved in neurodegenerative diseases which form fibrillar structures such as prion proteins, α-synuclein and amyloid beta. Also, we work on viral membrane proteins involved in replication complex formation, as well as on structural proteins forming capsids and envelopes. Another model to further explore the potential of solid-state NMR for the study of large and complex proteins is the bacterial ABC transporter BmrA.
Our lab has a strong focus on sample preparation techniques, and besides working on the overexpression, purification and characterization of specifically 13C/15N labeled protein models to implement and test protocols for NMR structure determination, we also develop alternative production in cell-free systems using wheat-germ extracts.
To advance our understanding of the molecular mechanisms underlying cellular biological processes, our structural studies are done in close collaboration with virologists and biologists involved in the functional analyses of the studied proteins in the cellular context.