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@ARTICLE{Schedler:1019401,
      author       = {Schedler, Benno and Yukhnovets, Olessya and Lindner,
                      Lennart and Meyer, Alida and Fitter, Jörg},
      title        = {{T}he {T}hermodynamic {F}ingerprints of {U}ltra-{T}ight
                      {N}anobody–{A}ntigen {B}inding {P}robed via {T}wo-{C}olor
                      {S}ingle-{M}olecule {C}oincidence {D}etection},
      journal      = {International journal of molecular sciences},
      volume       = {24},
      number       = {22},
      issn         = {1422-0067},
      address      = {Basel},
      publisher    = {Molecular Diversity Preservation International},
      reportid     = {FZJ-2023-05361},
      pages        = {16379 -},
      year         = {2023},
      abstract     = {Life on the molecular scale is based on a versatile
                      interplay of biomolecules, a featurethat is relevant for the
                      formation of macromolecular complexes. Fluorescence-based
                      two-colorcoincidence detection is widely used to
                      characterize molecular binding and was recently improvedby a
                      brightness-gated version which gives more accurate results.
                      We developed and establishedprotocols which make use of
                      coincidence detection to quantify binding fractions between
                      interactionpartners labeled with fluorescence dyes of
                      different colors. Since the applied technique is
                      intrinsicallyrelated to single-molecule detection, the
                      concentration of diffusing molecules for confocal
                      detectionis typically in the low picomolar regime. This
                      makes the approach a powerful tool for
                      determiningbi-molecular binding affinities, in terms of KD
                      values, in this regime. We demonstrated the reliabilityof
                      our approach by analyzing very strong nanobody-EGFP binding.
                      By measuring the affinity atdifferent temperatures, we were
                      able to determine the thermodynamic parameters of the
                      bindinginteraction. The results show that the ultra-tight
                      binding is dominated by entropic contributions.},
      cin          = {IBI-6},
      ddc          = {540},
      cid          = {I:(DE-Juel1)IBI-6-20200312},
      pnm          = {5352 - Understanding the Functionality of Soft Matter and
                      Biomolecular Systems (POF4-535)},
      pid          = {G:(DE-HGF)POF4-5352},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {38003569},
      UT           = {WOS:001113898000001},
      doi          = {10.3390/ijms242216379},
      url          = {https://juser.fz-juelich.de/record/1019401},
}