Výsledky vyhledávání - "Structure and function of the visual pigment rhodopsin"

Photoactivation of rhodopsin causes an increased hydrogen-deuterium exchange of buried peptide groups

Autor: Parshuram Rath, Willem J. DeGrip, Kenneth J. Rothschild

Publikováno v: Biophysical Journal, 74, pp. 192-198
Biophysical Journal, 74, 192-198

A key step in visual transduction is the light-induced conformational changes of rhodopsin that lead to binding and activation of the G-protein transducin. In order to explore the nature of these conformational changes, time-resolved Fourier transfor

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3c64846b4e7fec3d0db7077f9ced32d0
https://doi.org/10.1016/s0006-3495(98)77779-3

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Selective detergent-extraction from mixed detergent/lipid/protein micelles, using cyclodextrin inclusion compounds: A novel generic approach for the preparation of proteoliposomes

Autor: Grip, W.J. de, Oostrum, J. van, Bovee-Geurts, P.H.M.

Publikováno v: Biochemical Journal, 330, pp. 667-674
Biochemical Journal, 330, 667-674

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Externí odkaz: https://explore.openaire.eu/search/publication?articleId=dedup_wf_001::2fc323ea08ed96e99867ab6a73e9621e
https://hdl.handle.net/2066/265357

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Determination of a molecular torsional angle in the metarhodopsin-I photointermediate of rhodopsin by double-quantum solid-state NMR

Autor: Feng, X., Verdegem, P.J.E., Edén, M., Sandstrom, D., Lee, Y.K., Bovee-Geurts, P.H.M., Grip, W.J. de, Lugtenburg, J., Groot, H.J.M. de, Levitt, M.H.

Publikováno v: Journal of Biomolecular Nmr, 16, pp. 1-8
Journal of Biomolecular Nmr, 16, 1-8

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Externí odkaz: https://explore.openaire.eu/search/publication?articleId=dedup_wf_001::ce3b55bbc55832cc0abe41fc83254d5d
https://hdl.handle.net/2066/187038

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Retinylidene ligand structure in bovine rhodopsin, metarhodopsin-I, and 10-methylrhodopsin from internuclear distance measurements using 13C-labeling and 1-D rotational resonance MAS NMR

Autor: W.J. de Grip, H. J. M. de Groot, Johan Lugtenburg, Petra H. M. Bovee-Geurts, P. J. E. Verdegem

Publikováno v: Biochemistry
Biochemistry, 38(35), 11316-11324
Biochemistry, 38, pp. 11316-11324
Biochemistry, 38, 11316-11324

Rhodopsin is the G-protein coupled photoreceptor that initiates the rod phototransduction cascade in the vertebrate retina. Using specific isotope enrichment and magic angle spinning (MAS) NMR, we examine the spatial structure of the C10-C11=C12-C13-

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::21c3a16b785fda0062d3567e61d98317
https://pubmed.ncbi.nlm.nih.gov/10471281

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Macroscopic orientation of natural and model membranes for structural studies

Autor: W.J. de Grip, Clemens Glaubitz, G Grobner, G Choi, Jude A. Watts, Philip T. F. Williamson, Anthony Watts, Andrew M. Taylor

Publikováno v: Analytical Biochemistry, 254, pp. 132-138
Analytical Biochemistry, 254, 132-138
Analytical Biochemistry, 254, 1, pp. 132-138

One approach for obtaining high-resolution structural and functional information for biomembranes and their proteins is by static solid-state NMR of oriented systems. Here, a general procedure to align fully functional biological membranes containing

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::317fe5d1511fd4ecadcb877615c7303d
https://hdl.handle.net/2066/188914

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Direct determination of a molecular torsional angle in the membrane protein rhodopsin by solid-state NMR

Autor: X. Feng, H. J. M. de Groot, D. Sandström, P. J. E. Verdegem, Y. Lee, Johan Lugtenburg, Mattias Edén, Malcolm H. Levitt, W.J. de Grip, Petra H. M. Bovee-Geurts

Publikováno v: Journal of the American Chemical Society, 119, 6853-6857. Amer chemical soc
Journal of the American Chemical Society, 119(29), 6853-6857
Journal of the American Chemical Society, 119, 6853-6857
Journal of the American Chemical Society, 119, 29, pp. 6853-6857
Journal of the American Chemical Society, 119, pp. 6853-6857
Journal of the American Chemical Society

A solid-state NMR method (double-quantum heteronuclear local field NMR) is applied to a 13C2 labeled sample of the 41 kD integral membrane protein rhodopsin. The technique operates under magic-angle-spinning conditions, with good sensitivity and reso

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9658cc56a0f4b5198b529bbede0d059f
http://hdl.handle.net/2066/29353

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Photo-excitation by a half-carotenoid: Symbiosis between retinal and the visual protein opsin

Autor: Johan Lugtenburg, F. de Lange, W.J. de Grip, P. J. E. Verdegem, Petra Bovee

Publikováno v: Pure and Applied Chemistry, 69, 2091-2098. Blackwell science ltd
Pure and Applied Chemistry, 69, 2091-2098
Pure and Applied Chemistry, 69, pp. 2091-2098
Pure and Applied Chemistry, 69, 10, pp. 2091-2098

The visual process is initiated by photoactivation of a receptor protein, e.g. the vertebrate rod visual pigment rhodopsin. Upon absorption of light its chromophore, 11-cis retinal, stereoisomerizes to the all-trans (AT) state. This conformational ch

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7186fe0a81c930a0fd951e331ee9d86d
http://hdl.handle.net/2066/29147

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