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SUMMARY:NMR atomic-resolution structures of amyloids - Beat H. Meier (Labo
 ratory of Physical Chemistry\, ETH Zürich)
DTSTART:20180314T103000Z
DTEND:20180314T113000Z
UID:TALK102910@talks.cam.ac.uk
CONTACT:Florian Buhr
DESCRIPTION:Beat H. Meier\, Marielle Aulikki Wälti\, Francesco Ravotti\, 
 Anne Schütz\, Roland Riek (Laboratory of Physical Chemistry\, ETH Zürich
 )\n\nAnja Böckmann (Institut de Biologie et Chimie des Protéines\, Bases
  Moléculaires et Structurales des Systèmes Infectieux\, Labex Ecofect\, 
 UMR 5086 CNRS\, Université de Lyon)\n\nPeter Güntert (Institute of Bioph
 ysical Chemistry\, Center for Biomolecular Magnetic Resonance\, Goethe Uni
 versity Frankfurt am Main)\n\nStructure 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.\nWe will summarize\, at the example of th
 e amyloid beta Osaka mutant Aβ1-40 E22Δ involved in early-onset Alzheime
 r's disease which NMR data has to be recorded and how it can be analyzed i
 n order to yield reliable 3D structures of protein fibrils. Further applic
 ation of the established approaches to the structure of a polymorph of Aβ
 1-42 will be shown\, which has been further confirmed by an independent st
 udy\, with the same result. This is an important result as it confirms the
  maturity of the method to reproducible obtain virtually the same 3D struc
 tures for proteins showing highly similar chemical shift fingerprints. Sti
 ll\, it does not mean that this structure is the only existing structure o
 f Aβ1-42\, as we and others reported different polymorphs\, one indeed wi
 th an atomic resolution structure\, of this protein as well. I will also d
 iscuss hypotheses as to the structural bases of early onset.\n\n
LOCATION:Department of Chemistry\, Cambridge\, Unilever lecture theatre
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