Lay summary
A number of devastating diseases such as Alzheimer’s, Parkinson’s and prion diseases occur when proteins or fragments of proteins undergo structural changes into insoluble aggregates termed amyloid fibrils. These protein deposition diseases are collectively called amyloid diseases. Each of the amyloid diseases is associated with a disease-specific protein. Its conformational change from soluble form into amyloid fibrils is thought to be the direct cause of the disease in questions and the amyloid fibrils of this protein are a pathological hallmark of the diseases. For example, Alzheimer’s disease is associated with the progressive accumulation of amyloid deposits in the brain called plaques that can be identified under the microscope.
It is our long-term aim to determine the structure of the normal, intermediate and aggregated forms of a variety of amyloid proteins to define motifs associated with amyloid formation, toxicity or/and infectivity. The final goal is a detailed time-resolved description of the conformational switch of amyloid proteins and knowledge about their specific disease-associated properties.

Integral membrane proteins, constituting nearly 1/3 of eukaryotic genes, play central roles in cellular transport processes, intercellular signaling, and growth regulations. Furthermore, membrane proteins are the major drag targets of pharmaceutricla industries. However, of the ~30000 high-resolution protein structures known, only about 30 unique families of integral membrane proteins are represented - not one human membrane protein structure is known. This disparity is accounted for by two bottlenecks in membrane protein structure analysis: (i) high-yield protein production and (ii) 3D structure determination.
It is our long-term goal to advance structural biology of membrane proteins by solution NMR with special emphasis on structural and dynamic insights into GPCRs and ion channels on an atomic level. We will continue to apply Nuclear Magnetic Resonance (NMR) spectroscopy as a major technique towards this aim. Further technical developments will be undertaken to improve the quality of structures of membrane proteins.