These authors contributed equally to this work.
Zuschrift
Solution NMR Structure of Proteorhodopsin†
Article first published online: 27 OCT 2011
DOI: 10.1002/ange.201105648
Copyright © 2011 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim
Additional Information
How to Cite
Reckel, S., Gottstein, D., Stehle, J., Löhr, F., Verhoefen, M.-K., Takeda, M., Silvers, R., Kainosho, M., Glaubitz, C., Wachtveitl, J., Bernhard, F., Schwalbe, H., Güntert, P. and Dötsch, V. (2011), Solution NMR Structure of Proteorhodopsin. Angew. Chem., 123: 12148–12152. doi: 10.1002/ange.201105648
- †
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.
- ‡
These authors contributed equally to this work.
Publication History
- Issue published online: 7 DEC 2011
- Article first published online: 27 OCT 2011
- Manuscript Received: 9 AUG 2011
Funded by
- Deutsche Forschungsgemeinschaft. Grant Number: DO545/7-1
- European Drug Initiative on Channels and Transporters (EDICT). Grant Number: HEALTH-F4-2007-201924
- NIH. Grant Number: U54 GM094608
- Center for Biomolecular Magnetic Resonance (BMRZ)
- Cluster of Excellence Frankfurt
- Volkswagen Foundation
- Japan Society for the Promotion of Science
Keywords:
- Membranproteine;
- NMR-Spektroskopie;
- Proteorhodopsin;
- Strukturbiologie

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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