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@ARTICLE{Reinartz:893282,
      author       = {Reinartz, Ines and Sarter, Mona and Otten, Julia and
                      Höfig, Henning and Pohl, Martina and Schug, Alexander and
                      Stadler, Andreas M. and Fitter, Jörg},
      title        = {{S}tructural {A}nalysis of a {G}enetically {E}ncoded {FRET}
                      {B}iosensor by {SAXS} and {MD} {S}imulations},
      journal      = {Sensors},
      volume       = {21},
      number       = {12},
      issn         = {1424-8220},
      address      = {Basel},
      publisher    = {MDPI},
      reportid     = {FZJ-2021-02672},
      pages        = {4144 -},
      year         = {2021},
      abstract     = {Inspired by the modular architecture of natural signaling
                      proteins, ligand binding proteins are equipped with two
                      fluorescent proteins (FPs) in order to obtain Förster
                      resonance energy transfer (FRET)-based biosensors. Here, we
                      investigated a glucose sensor where the donor and acceptor
                      FPs were attached to a glucose binding protein using a
                      variety of different linker sequences. For three resulting
                      sensor constructs the corresponding glucose induced
                      conformational changes were measured by small angle X-ray
                      scattering (SAXS) and compared to recently published single
                      molecule FRET results (Höfig et al., ACS Sensors, 2018).
                      For one construct which exhibits a high change in energy
                      transfer and a large change of the radius of gyration upon
                      ligand binding, we performed coarse-grained molecular
                      dynamics simulations for the ligand-free and the
                      ligand-bound state. Our analysis indicates that a carefully
                      designed attachment of the donor FP is crucial for the
                      proper transfer of the glucose induced conformational change
                      of the glucose binding protein into a well pronounced FRET
                      signal change as measured in this sensor construct. Since
                      the other FP (acceptor) does not experience such a glucose
                      induced alteration, it becomes apparent that only one of the
                      FPs needs to have a well-adjusted attachment to the glucose
                      binding protein.},
      cin          = {IBG-1 / IBI-6 / JCNS-1 / IBI-8},
      ddc          = {620},
      cid          = {I:(DE-Juel1)IBG-1-20101118 / I:(DE-Juel1)IBI-6-20200312 /
                      I:(DE-Juel1)JCNS-1-20110106 / I:(DE-Juel1)IBI-8-20200312},
      pnm          = {2171 - Biological and environmental resources for
                      sustainable use (POF4-217)},
      pid          = {G:(DE-HGF)POF4-2171},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {34208740},
      UT           = {WOS:000667410700001},
      doi          = {10.3390/s21124144},
      url          = {https://juser.fz-juelich.de/record/893282},
}