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SUMMARY:Amyloids from the origin to the end of life - Professor Roland Rie
 k\, ETH Zurich
DTSTART:20170510T093000Z
DTEND:20170510T103000Z
UID:TALK72528@talks.cam.ac.uk
CONTACT:23027
DESCRIPTION:Protein aggregation is observed in many diseases including Alz
 heimer’s disease. These protein aggregates are termed amyloids. Amyloids
  are composed of pairs of tightly interacting\, many-stranded\, repetitive
 \, inter-molecular beta-sheets termed the cross-beta-sheet structure. Beca
 use of this structure\, amyloids can grow by recruitment of the same prote
 in while their repeat can transform a weak activity into a potent one thro
 ugh cooperativity and avidity. Thus\, an amyloid has the potential to repl
 icate itself\, and can be adaptive to its environment\, yielding eventuall
 y cell-to-cell transmissibility\, prion infectivity\, and toxicity. Here\,
  we discuss these structure-based properties within the context of Alzheim
 er’s disease and Parkinson’s disease from a structural perspective. In
  addition\, we discuss a potential role of amyloids in the origin of life 
 [1-3].\n\nReferences\n\n[1] J. Greenwald\, M. Friedmann\, Roland Riek\, An
 gewandte Chemie 53\, 11609 (2016).\n\n[2] M. Wälti\, F. Ravottie\, H. Ara
 l\, C. Glabe\, J. Wall\, A. Bockmann\, PO. Guntert\, B. Meier\, R. Riek\, 
 PNAS 113\, E4976 (2016).\n\n[3] R. Riek and D. Eisenberg\, Nature 539\, 22
 7 (2016).
LOCATION:Department of Chemistry\, Cambridge\, Unilever lecture theatre
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