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@PHDTHESIS{vonderHocht:1302,
      key          = {1302},
      othercontributors = {von der Hocht, Iris},
      title        = {{F}luorescence {S}pectroscopy of {R}ecoverin {F}unction and
                      {C}onformation},
      volume       = {4272},
      issn         = {0944-2952},
      school       = {Univ. Köln},
      type         = {Dr. (Univ.)},
      address      = {Jülich},
      publisher    = {Forschungszentrum Jülich GmbH Zentralbibliothek, Verlag},
      reportid     = {PreJuSER-1302, Juel-4272},
      series       = {Berichte des Forschungszentrums Jülich},
      pages        = {119 p.},
      year         = {2008},
      note         = {Record converted from VDB: 12.11.2012; Köln, Univ., Diss.,
                      2008},
      abstract     = {Recoverin is a neuronal calcium sensor protein
                      (NCS-protein) from the vertebrate photoreceptor which is
                      involved in light adaptation. Recoverin changes its
                      conformation upon sequential binding of two calcium ions.
                      This conformational change induces the extrusion of a
                      covalently attached myristoyl residue from a hydrophobic
                      binding pocket which enables Recoverin to interact with
                      lipid membranes (calcium-myristoyl switch). In this thesis,
                      I report on my investigation of Recoverin’s calcium
                      myristoyl switch, using a recently developed modification of
                      fluorescence correlation spectroscopy (FCS) that is called
                      dual-focus FCS (2fFCS). This method allows for measuring
                      absolute diffusion coefficients with an accuracy of better
                      than a few percent. Recoverin, and the Recoverin mutants
                      E85Q and E121Q which bind only one or no Ca$^{2+}$,
                      respectively, were labeled with the fluorescent dye
                      Alexa647. Differences in the hydrodynamic radius due to
                      conformational changes of Recoverin and its mutants upon
                      calcium binding were monitored by measuring the diffusion
                      coefficient of these molecules as a function of free calcium
                      concentration. The calcium dependent interaction of
                      Recoverin with lipid membranes was measured in solutions of
                      small unilamellar vesicles (SUVs) of different lipid
                      composition. Again, diffusion measurements were used to
                      determine the fraction of free and lipid-bound Recoverin
                      using the strongly different diffusion coefficients of both
                      fractions. To account for the fluorescence brightness
                      difference of the dye label when in solution and close to a
                      lipid membrane, a new three-photon correlation analysis was
                      developed and tested.},
      cin          = {INB-1},
      cid          = {I:(DE-Juel1)VDB804},
      pnm          = {Grundlagen für zukünftige Informationstechnologien},
      pid          = {G:(DE-Juel1)FUEK412},
      typ          = {PUB:(DE-HGF)11 / PUB:(DE-HGF)3},
      url          = {https://juser.fz-juelich.de/record/1302},
}