Interpretation of 100- and 360-MHz proton magnetic resonance spectra of retinal rod outer segment disk membranes.
@article{Brown1977InterpretationO1, title={Interpretation of 100- and 360-MHz proton magnetic resonance spectra of retinal rod outer segment disk membranes.}, author={M. F. Brown and George P. Miljanich and Edward A. Dratz}, journal={Biochemistry}, year={1977}, volume={16 12}, pages={ 2640-8 } }
Well resolved proton nuclear magnetic resonance ('H NMR) spectra of bovine retinal rod outer segment (ROS) disk membranes have been obtained at 100 and 360 MHz. The resolved IH resonances of the ROS membranes are due to phospholipids, with little contribution from rhodopsin. The spectra of both the ROS membranes and bilayer vesicles pre- pared from purified ROS phospholipids (liposomes) appear to represent a superposition of relatively sharp resonance components and a broad, underlying…
54 Citations
Proton, carbon-13, and phosphorus-31 NMR methods for the investigation of rhodopsin--lipid interactions in retinal rod outer segment membranes.
- Biology, ChemistryMethods in enzymology
- 1982
Retinal rod outer segment lipids form bilayers in the presence and absence of rhodopsin: a 31P NMR study
- Biology, ChemistryFEBS letters
- 1981
THE STRUCTURE OF RHODOPSIN AND ITS DISPOSITION IN THE ROD OUTER SEGMENT DISK MEMBRANE *
- Biology, ChemistryPhotochemistry and photobiology
- 1979
Experiments with membrane impermeable covalent labeling reagents and permeable analogues imply that rhodopsin has an aqueous surface on both sides of the membrane permeability harrier, and chemical labeling together with freeze fracture evidence indicates that r Rhodopsin is a transmembrane protein.
Proton and carbon-13 nuclear magnetic resonance studies of rhodopsin-phospholipid interactions.
- Biology, ChemistryBiochemistry
- 1979
Proton and carbon-13 nuclear magnetic resonance spectra of rhodopsin-phospholipid membrane vesicles and sonicated disk membranes suggest a membrane model in which the lipid molecules preferentially solvate the protein with the sn-1 chain, which the authors term an edge-on orientation.
Thermotropic behavior of retinal rod membranes and dispersions of extracted phospholipids
- BiologyThe Journal of Membrane Biology
- 2005
High sensitivity, differential scanning calorimetry studies of vovine retinal rod outer segment (ROS) disk membranes and aqueous dispersions of the extracted ROS phospholipids suggest that the thermotropic behavior reffects a gel-to-liquid crystalline transition, leading to lateral phase separation, involving those phosphatidylcholine (PC) molecules containing saturated fatty acylchains.
Rhodopsin-lipid associations in bovine rod outer segment membranes. Identification of immobilized lipid by spin-labels.
- BiologyBiochemistry
- 1979
Rhodopsin-lipid interactions have been studied in bovine rod outer segment (ROS) membranes by using spin-labels and parameters are useful when interpreting observations of the interactions between lipids and integral membrane proteins in structural terms.
Molecular exchange at the lipid-rhodopsin interface: spin-label electron spin resonance studies of rhodopsin-dimyristoylphosphatidylcholine recombinants.
- Biology, ChemistryBiochemistry
- 1987
The photoreceptor protein rhodopsin has been reconstituted with a single phospholipid species, dimyristoylphosphatidylcholine, at a range of different lipid/protein ratios, and the exchange rate at…
Interaction between spin‐labeled rhodopsin and spin‐labeled phospholipids in the retinal outer segment disc membranes
- Biology, ChemistryFEBS letters
- 1978
Dynamical and temperature-dependent effects of lipid-protein interactions. Application of deuterium nuclear magnetic resonance and electron paramagnetic resonance spectroscopy to the same reconstitutions of cytochrome c oxidase.
- Chemistry, BiologyBiochemistry
- 1981
At temperatures well above the phase transition of the pure lipid, the average orientational parameters derived from the 2H NMR spectra are independent of protein concentration and are the same as for the lipid alone.
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