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Literature DB >> 958369

Neutron diffraction studies of retinal rod outer segment membranes.

Abstract

Neutron diffraction measurements on isolated retinal rod outer segments show that most of the visual pigment protein, rhodopsin, is embedded in the hydrophobic core of the disk membrane. A very slight outward shift of protein at the cytoplasmic side of the membrane is associated with pigment bleaching.

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Year: 1976 PMID： 958369 DOI： 10.1038/262266a0

Source DB: PubMed Journal: Nature ISSN： 0028-0836 Impact factor: 49.962

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Cited

27 in total

1. The G protein-coupled receptor rhodopsin in the native membrane.

Authors: Dimitrios Fotiadis; Yan Liang; Slawomir Filipek; David A Saperstein; Andreas Engel; Krzysztof Palczewski
Journal: FEBS Lett Date: 2004-04-30 Impact factor: 4.124

Review 2. G protein-coupled receptor rhodopsin.

Authors: Krzysztof Palczewski
Journal: Annu Rev Biochem Date: 2006 Impact factor: 23.643

3. Opsin is present as dimers in COS1 cells: identification of amino acids at the dimeric interface.

Authors: Parvathi Kota; Philip J Reeves; Uttam L Rajbhandary; H Gobind Khorana
Journal: Proc Natl Acad Sci U S A Date: 2006-02-21 Impact factor: 11.205

4. Discussion to II. Light-induced conformational changes of the rhodopsin molecule.

Authors:
Journal: Biophys Struct Mech Date: 1977-06-29

5. The transducin cascade is involved in the light-induced structural changes observed by neutron diffraction on retinal rod outer segments.

Authors: T M Vuong; C Pfister; D L Worcester; M Chabre
Journal: Biophys J Date: 1987-10 Impact factor: 4.033

Neutron diffraction studies of retinal rod outer segment membranes.

1. The G protein-coupled receptor rhodopsin in the native membrane.

Review 2. G protein-coupled receptor rhodopsin.

3. Opsin is present as dimers in COS1 cells: identification of amino acids at the dimeric interface.

4. Discussion to II. Light-induced conformational changes of the rhodopsin molecule.

5. The transducin cascade is involved in the light-induced structural changes observed by neutron diffraction on retinal rod outer segments.

6. Birefringence measurements of structural inhomogeneities in Rana pipiens rod outer segments.

7. Structural interpretation of the birefringence gradient in retinal rod outer segments.

8. Diamagnetic anisotropy and orientation of alpha helix in frog rhodopsin and meta II intermediate.

9. Functional characterization of rhodopsin monomers and dimers in detergents.

10. Orientational behavior of phosphatidylcholine bilayers in the presence of aromatic amphiphiles and a magnetic field.