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Solution NMR Structure of Proteorhodopsin

Authors

  • Sina Reckel,

    1. Institute of Biophysical Chemistry and Center for Biomolecular Magnetic Resonance, Goethe University Frankfurt, Max-von-Laue Str. 9, 60438 Frankfurt (Germany)
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    • These authors contributed equally to this work.

  • Daniel Gottstein,

    1. Institute of Biophysical Chemistry and Center for Biomolecular Magnetic Resonance, Goethe University Frankfurt, Max-von-Laue Str. 9, 60438 Frankfurt (Germany)
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    • These authors contributed equally to this work.

  • Jochen Stehle,

    1. Institute for Organic Chemistry and Chemical Biology and Center for Biomolecular Magnetic Resonance, Goethe University Frankfurt, Max-von-Laue Str. 7–9, 60438 Frankfurt (Germany)
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  • Dr. Frank Löhr,

    1. Institute of Biophysical Chemistry and Center for Biomolecular Magnetic Resonance, Goethe University Frankfurt, Max-von-Laue Str. 9, 60438 Frankfurt (Germany)
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  • Dr. Mirka-Kristin Verhoefen,

    1. Institute of Physical and Theoretical Chemistry, Goethe University Frankfurt, Max-von-Laue Str. 7, 60438 Frankfurt (Germany)
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  • Dr. Mitsuhiro Takeda,

    1. Structural Biology Research Center, Nagoya University, Furo-cho, Chikusa-ku, 464-8601 (Japan)
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  • Robert Silvers,

    1. Institute for Organic Chemistry and Chemical Biology and Center for Biomolecular Magnetic Resonance, Goethe University Frankfurt, Max-von-Laue Str. 7–9, 60438 Frankfurt (Germany)
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  • Prof. Dr. Masatsune Kainosho,

    1. Structural Biology Research Center, Nagoya University, Furo-cho, Chikusa-ku, 464-8601 (Japan)
    2. Center for Priority Areas, Tokyo Metropolitan University, Hachioji, Tokyo 192-0397 (Japan)
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  • Prof. Dr. Clemens Glaubitz,

    1. Institute of Biophysical Chemistry and Center for Biomolecular Magnetic Resonance, Goethe University Frankfurt, Max-von-Laue Str. 9, 60438 Frankfurt (Germany)
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  • Prof. Dr. Josef Wachtveitl,

    1. Institute of Physical and Theoretical Chemistry, Goethe University Frankfurt, Max-von-Laue Str. 7, 60438 Frankfurt (Germany)
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  • Dr. Frank Bernhard,

    1. Institute of Biophysical Chemistry and Center for Biomolecular Magnetic Resonance, Goethe University Frankfurt, Max-von-Laue Str. 9, 60438 Frankfurt (Germany)
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  • Prof. Dr. Harald Schwalbe,

    1. Institute for Organic Chemistry and Chemical Biology and Center for Biomolecular Magnetic Resonance, Goethe University Frankfurt, Max-von-Laue Str. 7–9, 60438 Frankfurt (Germany)
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  • Prof. Dr. Peter Güntert,

    1. Institute of Biophysical Chemistry and Center for Biomolecular Magnetic Resonance, Goethe University Frankfurt, Max-von-Laue Str. 9, 60438 Frankfurt (Germany)
    2. Frankfurt Institute for Advanced Studies, Goethe University Frankfurt, Ruth-Moufang-Str.1, 60438 Frankfurt am Main (Germany)
    3. Center for Priority Areas, Tokyo Metropolitan University, Hachioji, Tokyo 192-0397 (Japan)
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  • Prof. Dr. Volker Dötsch

    Corresponding author
    1. Institute of Biophysical Chemistry and Center for Biomolecular Magnetic Resonance, Goethe University Frankfurt, Max-von-Laue Str. 9, 60438 Frankfurt (Germany)
    • Institute of Biophysical Chemistry and Center for Biomolecular Magnetic Resonance, Goethe University Frankfurt, Max-von-Laue Str. 9, 60438 Frankfurt (Germany)
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  • This work was supported by the Deutsche Forschungsgemeinschaft (grant number DO545/7-1 and SFB 807), the European Drug Initiative on Channels and Transporters (EDICT) contract number HEALTH-F4-2007-201924, the NIH (grant number U54 GM094608), the Center for Biomolecular Magnetic Resonance (BMRZ) and the Cluster of Excellence Frankfurt (Macromolecular Complexes). The [11,20-13C2]retinal was a kind gift of Johan Lugtenburg, Peter Verdegem (Leiden University), Neville McLean, Malcolm H. Levitt and Richard C. D. Brown (Southampton University). P.G. gratefully acknowledges financial support by the Lichtenberg program of the Volkswagen Foundation and by a Grant-in-Aid for Scientific Research of the Japan Society for the Promotion of Science.

Abstract

original image

Ein gelöstes Rätsel: Die mit Lösungs-NMR-Spektroskopie bestimmte Struktur der aus sieben transmembranären Helices gebildeten Protonenpumpe Proteorhodopsin wurde durch Kombination von Daten aus NOE-Experimenten und verstärkter paramagnetischer Relaxation erhalten (siehe Bild). Die Genauigkeit, mit der die Struktur aufgeklärt wurde, konnte durch dipolare Restkopplungen verbessert werden.

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