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@ARTICLE{Schneider:16612,
      author       = {Schneider, R. and Schumacher, M.C. and Mueller, H. and
                      Nand, D. and Klaukien, V. and Heise, H. and Riedel, D. and
                      Wolf, G. and Behrmann, E. and Raunser, S. and Seidel, R. and
                      Engelhard, M. and Baldus, M.},
      title        = {{S}tructural {C}haracterization of {P}olyglutamine
                      {F}ibrils by {S}olid-{S}tate {NMR} {S}pectroscopy},
      journal      = {Journal of molecular biology},
      volume       = {412},
      issn         = {0022-2836},
      address      = {Amsterdam [u.a.]},
      publisher    = {Elsevier},
      reportid     = {PreJuSER-16612},
      pages        = {121 - 136},
      year         = {2011},
      note         = {This work was supported by the Deutsche
                      Forschungsgemeinschaft (Grant RA 1781/1-1), the Max Planck
                      Society, the Fonds der chemischen Industrie (Grant 684052),
                      and Netherlands Organisation for Scientific Research (Grant
                      700.26.121). R.S. thanks the Deutsche Forschungsgemeinschaft
                      graduate school 782 "Spectroscopy and Dynamics of Molecular
                      Coils and Aggregates" for a PhD fellowship.},
      abstract     = {Protein aggregation via polyglutamine stretches occurs in a
                      number of severe neurodegenerative diseases such as
                      Huntington's disease. We have investigated fibrillar
                      aggregates of polyglutamine peptides below, at, and above
                      the toxicity limit of around 37 glutamine residues using
                      solid-state NMR and electron microscopy. Experimental data
                      are consistent with a dry fibril core of at least 70-80 Å
                      in width for all constructs. Solid-state NMR dipolar
                      correlation experiments reveal a largely β-strand character
                      of all samples and point to tight interdigitation of
                      hydrogen-bonded glutamine side chains from different sheets.
                      Two approximately equally frequent populations of glutamine
                      residues with distinct sets of chemical shifts are found,
                      consistent with local backbone dihedral angles compensating
                      for β-strand twist or with two distinct sets of side-chain
                      conformations. Peptides comprising 15 glutamine residues are
                      present as single extended β-strands. Data obtained for
                      longer constructs are most compatible with a superpleated
                      arrangement with individual molecules contributing
                      β-strands to more than one sheet and an antiparallel
                      assembly of strands within β-sheets.},
      keywords     = {Magnetic Resonance Spectroscopy: methods / Microscopy,
                      Electron / Peptides: chemical synthesis / Peptides:
                      chemistry / Peptides (NLM Chemicals) / polyglutamine (NLM
                      Chemicals) / J (WoSType)},
      cin          = {ICS-6},
      ddc          = {570},
      cid          = {I:(DE-Juel1)ICS-6-20110106},
      pnm          = {Funktion und Dysfunktion des Nervensystems / BioSoft:
                      Makromolekulare Systeme und biologische
                      Informationsverarbeitung},
      pid          = {G:(DE-Juel1)FUEK409 / G:(DE-Juel1)FUEK505},
      shelfmark    = {Biochemistry $\&$ Molecular Biology},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:21763317},
      UT           = {WOS:000294523300012},
      doi          = {10.1016/j.jmb.2011.06.045},
      url          = {https://juser.fz-juelich.de/record/16612},
}