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Photoreceptor rhodopsin: structural and conformational study of its chromophore 11‐ cis retinal in oriented membranes by deuterium solid state NMR
Author(s) -
Gröbner Gerhard,
Choi Gregory,
Burnett Ian J,
Glaubitz Clemens,
Verdegem Peter J.E,
Lugtenburg Johan,
Watts Anthony
Publication year - 1998
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(97)01591-3
Subject(s) - rhodopsin , polyene , chromophore , retinaldehyde , chemistry , retinal , solid state nuclear magnetic resonance , membrane , crystallography , stereochemistry , schiff base , nuclear magnetic resonance spectroscopy , photochemistry , nuclear magnetic resonance , biochemistry , physics
Rhodopsin is the retinal photoreceptor responsible for visual signal transduction. To determine the orientation and conformation of retinal within the binding pocket of this membrane bound receptor, an ab initio solid state 2 H NMR approach was used. Bovine rhodopsin containing 11‐ cis retinal, specifically deuterated at its methyl groups at the C 19 or C 20 position, was uniaxially oriented in DMPC bilayers. Integrity of the membranes and quality of alignment were monitored by 31 P NMR. Analysis of the obtained 2 H NMR spectra provided angles for the individual labelled chemical bond vectors leading to an overall picture for the three dimensional structure of the polyene chain of the chromophore in the protein binding pocket around the Schiff base attachment site.