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@ARTICLE{Weirich:821070,
      author       = {Weirich, Franziska and Gremer, Lothar and Mirecka, Ewa A.
                      and Schiefer, Stephanie and Hoyer, Wolfgang and Heise,
                      Henrike},
      title        = {{S}tructural {C}haracterization of {F}ibrils from
                      {R}ecombinant {H}uman {I}slet {A}myloid {P}olypeptide by
                      {S}olid-{S}tate {NMR}: {T}he {C}entral {FGAILS} {S}egment
                      {I}s {P}art of the β-{S}heet {C}ore},
      journal      = {PLoS one},
      volume       = {11},
      number       = {9},
      issn         = {1932-6203},
      address      = {Lawrence, Kan.},
      publisher    = {PLoS},
      reportid     = {FZJ-2016-06314},
      pages        = {e0161243},
      year         = {2016},
      abstract     = {Amyloid deposits formed from islet amyloid polypeptide
                      (IAPP) are a hallmark of type 2 diabetes mellitus and are
                      known to be cytotoxic to pancreatic β-cells. The molecular
                      structure of the fibrillar form of IAPP is subject of
                      intense research, and to date, different models exist. We
                      present results of solid-state NMR experiments on fibrils of
                      recombinantly expressed and uniformly 13C, 15N-labeled human
                      IAPP in the non-amidated, free acid form. Complete
                      sequential resonance assignments and resulting constraints
                      on secondary structure are shown. A single set of chemical
                      shifts is found for most residues, which is indicative of a
                      high degree of homogeneity. The core region comprises three
                      to four β-sheets. We find that the central 23-FGAILS-28
                      segment, which is of critical importance for amyloid
                      formation, is part of the core region and forms a β-strand
                      in our sample preparation. The eight N-terminal amino acid
                      residues of IAPP, forming a ring-like structure due to a
                      disulfide bridge between residues C2 and C7, appear to be
                      well defined but with an increased degree of flexibility.
                      This study supports the elucidation of the structural basis
                      of IAPP amyloid formation and highlights the extent of
                      amyloid fibril polymorphism.},
      cin          = {ICS-6},
      ddc          = {500},
      cid          = {I:(DE-Juel1)ICS-6-20110106},
      pnm          = {553 - Physical Basis of Diseases (POF3-553)},
      pid          = {G:(DE-HGF)POF3-553},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000383255600003},
      doi          = {10.1371/journal.pone.0161243},
      url          = {https://juser.fz-juelich.de/record/821070},
}