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@ARTICLE{Mohanty:519,
      author       = {Mohanty, S. and Meinke, J. and Zimmermann, O. and Hansmann,
                      U. H. E.},
      title        = {{S}imulation of {T}op7-{CF}r: a transient helix extension
                      guides folding},
      journal      = {Proceedings of the National Academy of Sciences of the
                      United States of America},
      volume       = {105},
      issn         = {0027-8424},
      address      = {Washington, DC},
      publisher    = {Academy},
      reportid     = {PreJuSER-519},
      pages        = {8004 - 8007},
      year         = {2008},
      note         = {Record converted from VDB: 12.11.2012},
      abstract     = {Protein structures often feature beta-sheets in which
                      adjacent beta-strands have large sequence separation. How
                      the folding process orchestrates the formation and correct
                      arrangement of these strands is not comprehensively
                      understood. Particularly challenging are proteins in which
                      beta-strands at the N and C termini are neighbors in a
                      beta-sheet. The N-terminal beta-strand is synthesized early
                      on, but it can not bind to the C terminus before the chain
                      is fully synthesized. During this time, there is a danger
                      that the beta-strand at the N terminus interacts with nearby
                      molecules, leading to potentially harmful aggregates of
                      incompletely folded proteins. Simulations of the C-terminal
                      fragment of Top7 show that this risk of misfolding and
                      aggregation can be avoided by a "caching" mechanism that
                      relies on the "chameleon" behavior of certain segments.},
      keywords     = {Computer Simulation / Peptide Fragments: chemistry /
                      Protein Folding / Protein Structure, Secondary / Proteins:
                      chemistry / Proteins: metabolism / Temperature /
                      Thermodynamics / Peptide Fragments (NLM Chemicals) /
                      Proteins (NLM Chemicals) / J (WoSType)},
      cin          = {NIC},
      ddc          = {000},
      cid          = {I:(DE-Juel1)NIC-20090406},
      pnm          = {Scientific Computing},
      pid          = {G:(DE-Juel1)FUEK411},
      shelfmark    = {Multidisciplinary Sciences},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:18408166},
      pmc          = {pmc:PMC2786944},
      UT           = {WOS:000256781800020},
      doi          = {10.1073/pnas.0708411105},
      url          = {https://juser.fz-juelich.de/record/519},
}