% IMPORTANT: The following is UTF-8 encoded.  This means that in the presence
% of non-ASCII characters, it will not work with BibTeX 0.99 or older.
% Instead, you should use an up-to-date BibTeX implementation like “bibtex8” or
% “biber”.

@ARTICLE{Kaimann:314,
      author       = {Kaimann, T. and Metzger, S. and Kuhlmann, K. and Brandt, B.
                      and Birkmann, E. and Höltje, H.-D. and Riesner, D.},
      title        = {{M}olecular {M}odel of an alpha-helical {P}rion {P}rotein
                      dimer and its monomeric subunits as derived from chemical
                      cross-linking and molecular modeling calculations},
      journal      = {Journal of molecular biology},
      volume       = {376},
      issn         = {0022-2836},
      address      = {Amsterdam [u.a.]},
      publisher    = {Elsevier},
      reportid     = {PreJuSER-314},
      pages        = {582 - 596},
      year         = {2008},
      note         = {Record converted from VDB: 12.11.2012},
      abstract     = {Prions are the agents of a series of lethal
                      neurodegenerative diseases. They are composed largely, if
                      not entirely, of the host-encoded prion protein (PrP), which
                      can exist in the cellular isoform PrP(C) and the
                      pathological isoform PrP(Sc). The conformational change of
                      the alpha-helical PrP(C) into beta-sheet-rich PrP(Sc) is the
                      fundamental event of prion disease. The transition of
                      recombinant PrP from a PrP(C)-like into a PrP(Sc)-like
                      conformation can be induced in vitro by submicellar
                      concentrations of SDS. An alpha-helical dimer was identified
                      that might represent either the native state of PrP(C) or
                      the first step from the monomeric PrP(C) to highly
                      aggregated PrP(Sc). In the present study, the molecular
                      structure of these dimers was analyzed by introducing
                      covalent cross-links using 1-ethyl-3-(3-dimethylaminopropyl)
                      carbodiimide. Inter- and intramolecular bonds between
                      directly neighboured amino groups and carboxy groups were
                      generated. The bonds formed in PrP dimers of recombinant PrP
                      (90-231) were identified by tryptic digestion and subsequent
                      mass spectrometric analysis. Intra- and intermolecular
                      cross-links between N-terminal glycine and three acidic
                      amino acid side chains in the globular part of PrP were
                      identified, showing the N-terminal amino acids (90-124) are
                      not as flexible as known from NMR analysis. When the
                      cross-linked sites were used as structural constraint,
                      molecular modeling calculations yielded a structural model
                      for PrP dimer and its monomeric subunit, including the
                      folding of amino acids 90-124 in addition to the known
                      structure. Molecular dynamics of the structure after release
                      of the constraint indicated an intrinsic stability of the
                      domain of amino acids 90-124.},
      keywords     = {Amino Acids, Acidic: chemistry / Animals / Circular
                      Dichroism / Computer Simulation / Cricetinae / Cross-Linking
                      Reagents: chemistry / Dimerization / Mesocricetus / Models,
                      Molecular / Nuclear Magnetic Resonance, Biomolecular /
                      Prions: chemistry / Prions: genetics / Prions: metabolism /
                      Protein Conformation / Protein Isoforms: chemistry / Protein
                      Isoforms: metabolism / Protein Structure, Secondary /
                      Recombinant Proteins: chemistry / Recombinant Proteins:
                      metabolism / Spectrometry, Mass, Electrospray Ionization /
                      Tandem Mass Spectrometry / Trypsin: pharmacology / Amino
                      Acids, Acidic (NLM Chemicals) / Cross-Linking Reagents (NLM
                      Chemicals) / Prions (NLM Chemicals) / Protein Isoforms (NLM
                      Chemicals) / Recombinant Proteins (NLM Chemicals) / Trypsin
                      (NLM Chemicals) / J (WoSType)},
      cin          = {INB-2},
      ddc          = {570},
      cid          = {I:(DE-Juel1)VDB805},
      pnm          = {Funktion und Dysfunktion des Nervensystems},
      pid          = {G:(DE-Juel1)FUEK409},
      shelfmark    = {Biochemistry $\&$ Molecular Biology},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:18158160},
      UT           = {WOS:000253554700024},
      doi          = {10.1016/j.jmb.2007.11.035},
      url          = {https://juser.fz-juelich.de/record/314},
}