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NMR atomic-resolution structures of amyloids

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Beat H. Meier, Marielle Aulikki Wälti, Francesco Ravotti, Anne Schütz, Roland Riek (Laboratory of Physical Chemistry, ETH Z ürich)

Anja Böckmann (Institut de Biologie et Chimie des Protéines, Bases Moléculaires et Structurales des Systèmes Infectieux, Labex Ecofect, UMR 5086 CNRS , Université de Lyon)

Peter Güntert (Institute of Biophysical Chemistry, Center for Biomolecular Magnetic Resonance, Goethe University Frankfurt am Main)

Structure determination of amyloids by solid-state NMR is a powerful but also tricky method. In this contribution, we focus on details of the NMR spectroscopy employed and critical points to be considered for data analysis. We will summarize, at the example of the amyloid beta Osaka mutant Aβ1-40 E22 Δ involved in early-onset Alzheimer’s disease which NMR data has to be recorded and how it can be analyzed in order to yield reliable 3D structures of protein fibrils. Further application of the established approaches to the structure of a polymorph of Aβ1-42 will be shown, which has been further confirmed by an independent study, with the same result. This is an important result as it confirms the maturity of the method to reproducible obtain virtually the same 3D structures for proteins showing highly similar chemical shift fingerprints. Still, it does not mean that this structure is the only existing structure of Aβ1-42, as we and others reported different polymorphs, one indeed with an atomic resolution structure, of this protein as well. I will also discuss hypotheses as to the structural bases of early onset.

This talk is part of the Biophysical Seminars series.

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