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@ARTICLE{Loritz:15800,
      author       = {Loritz, H.M. and Kirchgeßner, N. and Born, S. and
                      Hoffmann, B. and Merkel, R.},
      title        = {{M}echamical {S}trength of {S}pecific {B}onds {A}cting
                      {I}solated or in {P}airs: {A} {C}ase {S}tudy on {E}ngineered
                      {P}roteins},
      journal      = {The journal of physical chemistry / B},
      volume       = {115},
      issn         = {1520-6106},
      address      = {Washington, DC},
      publisher    = {Soc.},
      reportid     = {PreJuSER-15800},
      pages        = {2582 - 2592},
      year         = {2011},
      note         = {Record converted from VDB: 12.11.2012},
      abstract     = {The dynamic strength of multiple specific bonds exposed to
                      external mechanical force is of significant interest for the
                      understanding of biological adhesion. Exploiting the
                      well-established FLAG tag technology, we engineered model
                      proteins exhibiting no, one, or two identical binding sites
                      for a monoclonal antibody. Bonds between these engineered
                      proteins and the antibody were studied with dynamic force
                      spectroscopy. On single bonds between a FLAG-tag and the
                      antibody, we observed two regimes corresponding to two
                      different activated complexes, that is, two intermediate
                      states along the reaction path for bond breakage. Dynamic
                      force spectroscopy on double bonds showed the same two
                      regimes. The actual yield forces of double bonds slightly
                      exceeded those of single bonds. A simplified kinetic model
                      with analytical solutions was developed and used to
                      interpret the measured spectra.},
      keywords     = {Algorithms / Antibodies, Monoclonal: chemistry /
                      Antibodies, Monoclonal: immunology / Antibody Affinity /
                      Biomechanics / Green Fluorescent Proteins: genetics /
                      Kinetics / Models, Chemical / Peptides: chemistry /
                      Peptides: genetics / Peptides: immunology / Probability /
                      Protein Binding / Protein Engineering / Recombinant
                      Proteins: chemistry / Recombinant Proteins: genetics /
                      Recombinant Proteins: immunology / Spectrum Analysis:
                      methods / Statistical Distributions / Antibodies, Monoclonal
                      (NLM Chemicals) / Peptides (NLM Chemicals) / Recombinant
                      Proteins (NLM Chemicals) / Green Fluorescent Proteins (NLM
                      Chemicals) / FLAG peptide (NLM Chemicals) / J (WoSType)},
      cin          = {ICS-7},
      ddc          = {530},
      cid          = {I:(DE-Juel1)ICS-7-20110106},
      pnm          = {BioSoft: Makromolekulare Systeme und biologische
                      Informationsverarbeitung},
      pid          = {G:(DE-Juel1)FUEK505},
      shelfmark    = {Chemistry, Physical},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:21355605},
      UT           = {WOS:000288401100013},
      doi          = {10.1021/jp108280q},
      url          = {https://juser.fz-juelich.de/record/15800},
}