Direct determination of a molecular torsional angle in the membrane protein rhodopsin by solid-state NMR
| Autor: | X. Feng, H. J. M. de Groot, D. Sandström, P. J. E. Verdegem, Y. Lee, Johan Lugtenburg, Mattias Edén, Malcolm H. Levitt, W.J. de Grip, Petra H. M. Bovee-Geurts |
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| Jazyk: | angličtina |
| Rok vydání: | 1997 |
| Předmět: |
biology
Structure and function of the visual pigment rhodopsin Chemistry Resolution (electron density) General Chemistry Biochemistry Catalysis Crystallography Colloid and Surface Chemistry Planar Membrane protein Heteronuclear molecule Solid-state nuclear magnetic resonance Rhodopsin biology.protein Structuur en functie van rhodopsine Local field Integral membrane protein GeneralLiterature_REFERENCE(e.g. dictionaries encyclopedias glossaries) |
| Zdroj: | Journal of the American Chemical Society, 119, 6853-6857. Amer chemical soc Journal of the American Chemical Society, 119(29), 6853-6857 Journal of the American Chemical Society, 119, 6853-6857 Journal of the American Chemical Society, 119, 29, pp. 6853-6857 Journal of the American Chemical Society, 119, pp. 6853-6857 Journal of the American Chemical Society |
| ISSN: | 0002-7863 |
| Popis: | A solid-state NMR method (double-quantum heteronuclear local field NMR) is applied to a 13C2 labeled sample of the 41 kD integral membrane protein rhodopsin. The technique operates under magic-angle-spinning conditions, with good sensitivity and resolution, and allows a direct determination of molecular torsional angles, without estimating internuclear distances. In rhodopsin, we determine the H−C10−C11−H torsional angle of the retinylidene chromophore to be 160 ± 10°, indicating a significant deviation from the planar 10-11-s-trans conformation. Double-quantum heteronuclear local field NMR is shown to be a feasible method for the accurate determination of local molecular conformation in large molecular systems which are unsuitable for crystallography. |
| Databáze: | OpenAIRE |
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