% 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{Meinke:55426,
      author       = {Meinke, J. and Hansmann, U.},
      title        = {{A}ggregation of {B}eta-{A}myloid {F}ragments},
      journal      = {The journal of chemical physics},
      volume       = {126},
      issn         = {0021-9606},
      address      = {Melville, NY},
      publisher    = {American Institute of Physics},
      reportid     = {PreJuSER-55426},
      pages        = {014706},
      year         = {2007},
      note         = {Record converted from VDB: 12.11.2012},
      abstract     = {The authors study the folding and aggregation of six chains
                      of the beta-amyloid fragment 16-22 using Monte Carlo
                      simulations. While the isolated fragment prefers a helical
                      form at room temperature, in the system of six interacting
                      fragments one observes both parallel and antiparallel beta
                      sheets below a crossover temperature T(x) approximately
                      equal to 420 K. The antiparallel sheets have lower energy
                      and are therefore more stable. Above the nucleation
                      temperature the aggregate quickly dissolves into widely
                      separated, weakly interacting chains.},
      keywords     = {Amyloid beta-Peptides: chemistry / Amyloid beta-Peptides:
                      ultrastructure / Binding Sites / Computer Simulation /
                      Dimerization / Models, Chemical / Models, Molecular / Monte
                      Carlo Method / Multiprotein Complexes: chemistry /
                      Multiprotein Complexes: ultrastructure / Peptide Fragments:
                      chemistry / Peptide Fragments: ultrastructure / Protein
                      Binding / Protein Conformation / Protein Folding /
                      Temperature / Amyloid beta-Peptides (NLM Chemicals) /
                      Multiprotein Complexes (NLM Chemicals) / Peptide Fragments
                      (NLM Chemicals) / amyloid beta-protein (16-22) (NLM
                      Chemicals) / J (WoSType)},
      cin          = {NIC},
      ddc          = {540},
      cid          = {I:(DE-Juel1)NIC-20090406},
      pnm          = {Scientific Computing},
      pid          = {G:(DE-Juel1)FUEK411},
      shelfmark    = {Physics, Atomic, Molecular $\&$ Chemical},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:17212510},
      UT           = {WOS:000243380000031},
      doi          = {10.1063/1.2423013},
      url          = {https://juser.fz-juelich.de/record/55426},
}