G. Grobner et al., PHOTORECEPTOR RHODOPSIN - STRUCTURAL AND CONFORMATIONAL STUDY OF ITS CHROMOPHORE 11-CIS RETINAL IN ORIENTED MEMBRANES BY DEUTERIUM SOLID-STATE NMR, FEBS letters, 422(2), 1998, pp. 201-204
Rhodopsin is the retinal photoreceptor responsible for visual signal t
ransduction. To determine the orientation and conformation of retinal
within the binding pocket of this membrane bound receptor, an ab initi
o solid state H-2 NMR approach was used. Bovine rhodopsin containing I
l-cis retinal, specifically deuterated at its methyl groups at the C-1
9 or C-20 position, was uniaxially oriented in DMPC bilayers. Integrit
y of the membranes and quality of alignment were monitored by P-31 NMR
. Analysis of the obtained H-2 NMR spectra provided angles for the ind
ividual labelled chemical bond vectors leading to an overall picture f
or the three dimensional structure of the polyene chain of the chromop
hore in the protein binding pocket around the Schiff base attachment s
ite. (C) 1998 Federation of European Biochemical Societies.