
Bamberg, Ernst (P10)
Max Planck Institute of
Biophysics, Frankfurt a.M.
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Fendler, Klaus (P10)
Max Planck Institute of
Biophysics, Frankfurt a.M.
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Forrest, Lucy (P8)
Computational Structural Biology
Max Planck Institute of
Biophysics, Frankfurt a.M.
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Gottschalk, Alexander (P11)
Institute of Biochemistry
Goethe-University Frankfurt a.M.
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Mäntele, Werner (P5)
Institute of Biophysics
Goethe-University Frankfurt a.M.
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Prisner, Thomas (P7)
Institute of Physical and Theoretical Chemistry &
Center of Biomolecular
Magnetic Resonance
Goethe-University Frankfurt a.M.
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Wachtveitl, Josef (P12)
Institute of Biophysics &
Institute of Physical and
Theoretical Chemistry
Goethe-University Frankfurt a.M.
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Mäntele (P5) | Prisner (P7) | Forrest (P8) | Fendler/Bamberg (P10) | Gottschalk (P11) | Wachtveitl (P12)
In contrast to transporters, channel proteins do not transform energy but act as selective pores in response to stimuli such as light or membrane potential. A small number of 3D structures of ion channels have been solved, which – together with other data – indicate the existence of distinct conformational states.
Voltage-dependent states of the tetrameric K+ channel KvAP will be determined in lipid bilayers by dipolar EPR spectroscopy. The methodological developments needed for this project will be directly applied to other transporters within this SFB. Recently, a novel class of ion channels, the light gated channelrhodopsins (ChR1, 2) has been discovered and was described. These channels represent a long sought-after and unique tool for neurobiological applications because they allow the light-induced depolarization of cells as demonstrated in excitable cells in transgenic animals by induction of light dependent behavior.