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@PHDTHESIS{Glck:837200,
      author       = {Glück, Julian Marius},
      title        = {{L}igand interaction analysis of membrane-anchored
                      proteins},
      volume       = {31},
      school       = {Universität Düsseldorf},
      type         = {Dr.},
      address      = {Jülich},
      publisher    = {Forschungszentrum Jülich GmbH Zentralbibliothek, Verlag},
      reportid     = {FZJ-2017-06179},
      isbn         = {978-3-89336-683-5},
      series       = {Schriften des Forschungszentrums Jülich. Reihe Gesundheit
                      / Health},
      pages        = {VIII, 87 S : graph. Darst},
      year         = {2010},
      note         = {Keine Online-Freischaltung; Universität Düsseldorf,
                      Diss., 2010},
      abstract     = {Diverse cellular functions including signaling, transport,
                      recognition and stability are performed by integral membrane
                      proteins (IMPs). For this reason various studies focus on
                      this prominent group of proteins. IMPs contain hydrophobic
                      regions that restrict solubility in aqueous solutions.
                      Unfortunately, many biophysical techniques require soluble
                      analytes. Therefore, if IMPs are supposed to be studied they
                      need to be maintained in a solubilized and functional state.
                      This can be accomplished with different approaches that
                      mimic the physicochemical properties of a membrane. In this
                      work a novel membrane mimic termed nanodisc was applied for
                      the study of an IMP. Nanodiscs are detergent-free model
                      membranes that consist of ∼150 lipid molecules arranged as
                      a bilayer. The discoidal lipid core is encircled by two
                      copies of an amphipathic α-helical protein in a belt-like
                      manner. A single disc possesses a diameter of ∼10 nm and a
                      lipid-dependent thickness of ∼5 nm. The aim of the current
                      thesis was the evaluation of nanodiscs as model membrane in
                      structural and interaction analyses of IMPs. For this
                      purpose a protocol enabling the successful incorporation of
                      CD4mut, a truncated human CD4 (cluster of differentiation 4)
                      receptor comprising transmembrane and cytoplasmic domains,
                      was established. Structural studies by solution NMR
                      spectroscopy on nanodisc embedded $^{13}$C/$^{15}$N-labeled
                      CD4mut showed reasonably dispersed protein and lipid
                      resonances in aliphatic $^{1}$H-$^{13}$C HSQC spectra. The
                      $^{1}$H line widths are in the range of 15 to 30 Hz. In
                      comparison with globular proteins of ∼150 kDa, similar to
                      the molecular weight of a nanodisc, significantly broader
                      lines are expected. These results demonstrated for the first
                      time that IMPs in nanodiscs are amenable to liquid-state NMR
                      spectroscopy. Furthermore, applicability of IMP containing
                      nanodiscs as analytes in surface plasmon resonance (SPR)
                      technology was examined. SPR measurements were conducted
                      with an antibody directed against oligohistidines (His)
                      immobilized on the sensor chip and either His-Ubiquitin or
                      His-Ubiquitin fused to nanodisc-embedded CD4mut as analyte
                      (loaded nanodisc). In both cases similar affinities (KD)
                      close to 10 nM were determined. This is expected as both
                      interactions should be governed by the same affinity between
                      His-tag [...]},
      keywords     = {Membranproteine (gnd) / Membrantransport (gnd)},
      cin          = {ISB-3},
      ddc          = {570},
      cid          = {I:(DE-Juel1)VDB942},
      pnm          = {899 - ohne Topic (POF3-899)},
      pid          = {G:(DE-HGF)POF3-899},
      typ          = {PUB:(DE-HGF)3 / PUB:(DE-HGF)11},
      url          = {https://juser.fz-juelich.de/record/837200},
}