Martina Huber, Department of Physics, Huygens-Kamerlingh Onnes Laboratory, Leiden University, The Netherlands

Electron Paramagnetic Resonance Approaches to Intrinsically Disordered Proteins and Aggregation Processes of Amyloid Proteins

Intrinsically Disordered Proteins (IDP’s) gained notoriety by being involved in diseases, mostly of the neurodegenerative kind. Key molecular processes in amyloid disease are: Amyloid-protein aggregation, amyloid membrane interaction including possible membrane damage and interactions with metal ions. Here we describe how advanced electron paramagnetic resonance techniques can elucidate these processes, using human α-Synuclein (αS) as an example. This protein combines both functional and pathological aspects of IDP’s, as it is a natural protein in the brain, where it associates with neuronal junctions (synapses), however, with so far unexplained function.  It is also the major component of the plaques (Lewy bodies) in the brains affected by Parkinson’s disease, where αS has a β-sheet conformation. The cartoon shows its various guises.

While the above examples derive from a biochemical question, the approaches are equally useful to determine size and interactions in nano-objects derived from other sources.

Host: Professor Daniel Otzen, iNANO & Dept. of Molecular Biology and Genetics, Aarhus University