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@ARTICLE{Fitter:4685,
      author       = {Fitter, J.},
      title        = {{T}he perspective of studying multi-domain protein folding},
      journal      = {Cellular and molecular life sciences},
      volume       = {66},
      issn         = {1420-682X},
      address      = {Basel},
      publisher    = {Birkhäuser},
      reportid     = {PreJuSER-4685},
      pages        = {1672 - 1681},
      year         = {2009},
      note         = {Record converted from VDB: 12.11.2012},
      abstract     = {Most of fundamental studies on protein folding have been
                      performed with small globular proteins consisting of a
                      single domain. In vitro many of these proteins are well
                      characterized by a reversible two-state folding scheme.
                      However, the majority of proteins in the cell belong to the
                      class of larger multi-domain proteins that often unfold
                      irreversibly under in vitro conditions. This makes folding
                      studies difficult or even impossible. In spite of these
                      problems for many multi-domain proteins, folding has been
                      investigated by classical refolding. Co-translational
                      folding of nascent polypeptide chains when synthesized by
                      ribosomes has also been studied. Single molecule techniques
                      represent a promising approach for future studies on the
                      folding of multi-domain proteins, and tremendous advances
                      have been made in these techniques in recent years. In
                      particular, fluorescence-based methods can contribute
                      significantly to an understanding of the fundamental
                      principles of multi-domain protein folding.},
      keywords     = {Animals / Humans / Models, Molecular / Protein Folding /
                      Protein Structure, Tertiary / Proteins: chemistry /
                      Spectrometry, Fluorescence / Proteins (NLM Chemicals) / J
                      (WoSType)},
      cin          = {ISB-2},
      ddc          = {570},
      cid          = {I:(DE-Juel1)ISB-2-20090406},
      pnm          = {Programm Biosoft},
      pid          = {G:(DE-Juel1)FUEK443},
      shelfmark    = {Biochemistry $\&$ Molecular Biology / Cell Biology},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:19183848},
      UT           = {WOS:000268003600004},
      doi          = {10.1007/s00018-009-8771-9},
      url          = {https://juser.fz-juelich.de/record/4685},
}