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@PHDTHESIS{Cukkemane:1301,
      author       = {Cukkemane, Abhishek},
      title        = {{S}tructural and functional studies of a prokaryotic cyclic
                      nucleotide-gated channel},
      volume       = {4270},
      issn         = {0944-2952},
      school       = {Univ. Köln},
      type         = {Dr. (Univ.)},
      address      = {Jülich},
      publisher    = {Forschungszentrum Jülich GmbH Zentralbibliothek, Verlag},
      reportid     = {PreJuSER-1301, Juel-4270},
      series       = {Berichte des Forschungszentrums Jülich},
      pages        = {VIII, 114 p.},
      year         = {2008},
      note         = {Record converted from VDB: 12.11.2012; Köln, Univ., Diss.,
                      2007},
      abstract     = {Ion channels gated by cyclic nucleotides have crucial roles
                      in cardiac and neuronal excitability and in signal
                      transduction of sensory neurons. On binding cyclic
                      nucleotides these channels are activated, which results an
                      increase in membrane conductance. Although a lot of
                      information is available on the function of these channel
                      proteins, the molecular events that relay ligand binding to
                      channel activation is not well understood. Here, I studied
                      ligand binding of prokaryotic cyclic nucleotide-activated
                      K$^{+}$ channels. One of them, the mlCNG channel from the
                      nitrogen-fixing bacterium Mesorhizobium loti was suitable
                      for biophysical characterization. One of the key questions
                      that I worked on was how gating of the channel affects its
                      ligand binding properties? I performed ligand binding
                      studies on the tetrameric mlCNG protein and its isolated
                      cyclic nucleotide-binding domain (CNBD). Affinity of cyclic
                      nucleotides to the full-length mlCNG protein and to the CNBD
                      was determined using spectroscopic methods. Both, the mlCNG
                      channel and the CNBD bind cAMP in a non-cooperative manner
                      with similar binding affinity. These results indicate that
                      either no appreciable binding energy is required for
                      activation, or the conformational change in the CNBD is the
                      activation step itself. Crystallography experiments were
                      performed on the mlCNG channel. Two-dimensional crystals
                      were obtained in which the channel proteins were ordered in
                      a square lattice. The channel proteins were assembled as
                      tetramers and were arranged in a head-to tail fashion. The
                      crystal diffracts to 15 Å. This is an excellent starting
                      condition for future work to eventually obtain a structure
                      at atomic resolution.},
      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/1301},
}