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@ARTICLE{Mller:173322,
      author       = {Müller, Henrik and Brener, Oleksandr and Andreoletti,
                      Olivier and Piechatzek, Timo and Willbold, Dieter and
                      Legname, Giuseppe and Heise, Henrike},
      title        = {{P}rogress towards structural understanding of infectious
                      sheep {P}r{P}-amyloid},
      journal      = {Prion},
      volume       = {8},
      number       = {5},
      issn         = {1933-690X},
      address      = {Austin, Tex.},
      publisher    = {Landes Bioscience},
      reportid     = {FZJ-2014-06732},
      pages        = {344-358},
      year         = {2014},
      abstract     = {The still elusive structural difference of non-infectious
                      and infectious amyloid of the mammalian prion protein (PrP)
                      is a major pending milestone in understanding
                      protein-mediated infectivity in neurodegenerative diseases.
                      Preparations of PrP-amyloid proven to be infectious have
                      never been investigated with a high-resolution technique.
                      All available models to date have been based on
                      low-resolution data. Here, we establish protocols for the
                      preparation of infectious samples of full-length recombinant
                      (rec) PrP¡amyloid in NMR-sufficient amounts by spontaneous
                      fibrillation and seeded fibril growth from brain extract. We
                      link biological and structural data of infectious
                      recPrP-amyloid, derived from bioassays, atomic force
                      microscopy, and solid-state NMR spectroscopy. Our data
                      indicate a semi-mobile N‑terminus, some residues with
                      secondary chemical shifts typical of α‑helical secondary
                      structure in the middle part between ~115 to ~155, and a
                      distinct β‑sheet core C‑terminal of residue ~155. These
                      findings are not in agreement with all current models for
                      PrP-amyloid. We also provide evidence that samples seeded
                      from brain extract may not differ in the overall arrangement
                      of secondary structure elements, but rather in the
                      flexibility of protein segments outside the β-core region.
                      Taken together, our protocols provide an essential basis for
                      the high-resolution characterization of non-infectious and
                      infectious PrP-amyloid in the near future.},
      cin          = {ICS-6},
      ddc          = {570},
      cid          = {I:(DE-Juel1)ICS-6-20110106},
      pnm          = {452 - Structural Biology (POF2-452)},
      pid          = {G:(DE-HGF)POF2-452},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000348376700004},
      doi          = {10.4161/19336896.2014.983754},
      url          = {https://juser.fz-juelich.de/record/173322},
}