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Literature DB >> 890046

Transient light-induced conformational changes in rhodopsin.

Abstract

Arguments are presented which support the possibility that the unfolding of the rhodopsin molecule during photolysis up to the stage of metarhodopsin II is followed by a spontaneous refolding of the protein, once the isomerized retinaldehyde has left its original binding site. Such a transient conformational change might imply a very similar conformation for rhodopsin and opsin, apart from the presence of the chromophore.

Entities: Chemical Gene

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Year: 1977 PMID： 890046 DOI： 10.1007/bf00535803

Source DB: PubMed Journal: Biophys Struct Mech ISSN： 0340-1057

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References

11 in total

1. Photoregeneration of rhodopsin and isorhodopsin from metarhodopsin III in the frog retina.

Authors: T Reuter
Journal: Vision Res Date: 1976 Impact factor: 1.886

2. TAUTOMERIC FORMS OF METARHODOPSIN.

Authors: R G MATTHEWS; R HUBBARD; P K BROWN; G WALD
Journal: J Gen Physiol Date: 1963-11 Impact factor: 4.086

3. Existence of a beta-ionone ring-binding site in the rhodopsin molecule.

Authors: H Matsumoto; T Yoshizawa
Journal: Nature Date: 1975-12-11 Impact factor: 49.962

4. The light reaction in the bleaching of rhodopsin.

Authors: G WALD; J DURELL; C C ST GEORGE
Journal: Science Date: 1950-02-17 Impact factor: 47.728

5. Biochemical aspects of the visual process. XXXIV. Relation between sulfhydryl groups and properties of rhodopsin studied by means of methylmercuric iodide.

Authors: F J Daemen; P J Van Breugel; P A Jansen; S L Bonting
Journal: Biochim Biophys Acta Date: 1976-12-22

6. Biochemical aspects of the visual process. XXVI. Binding site and migration of retinaldehyde during rhodopsin photolysis.

Authors: J P Rotmans; F J Daemen; S L Bonting
Journal: Biochim Biophys Acta Date: 1974-07-25

Transient light-induced conformational changes in rhodopsin.

1. Photoregeneration of rhodopsin and isorhodopsin from metarhodopsin III in the frog retina.

2. TAUTOMERIC FORMS OF METARHODOPSIN.

3. Existence of a beta-ionone ring-binding site in the rhodopsin molecule.

4. The light reaction in the bleaching of rhodopsin.

5. Biochemical aspects of the visual process. XXXIV. Relation between sulfhydryl groups and properties of rhodopsin studied by means of methylmercuric iodide.

6. Biochemical aspects of the visual process. XXVI. Binding site and migration of retinaldehyde during rhodopsin photolysis.

7. Biochemical aspects of the visual process. 23. Sulfhydryl groups and rhodopsin photolysis.

8. Biochemical aspects of the visual process. XXII. Amino group modification in bovine rod photoreceptor membranes.

9. Molecular basis of visual excitation.

10. The role of sulfhydryl groups in the bleaching and synthesis of rhodopsin.