A review is given of the use of nuclear magnetic resonance (NMR) spectroscopy to study bacteriorhodopsin and bovine rhodopsin. Solution and solid-state approaches are included. The studies of the bacterial proton pump examine the chromophore, the peptide backbone, and the protein side chains. The studies of the bovine visual pigment are limited to the chromophore. Various forms of each pigment are considered. Both structural and dynamic features are addressed.
Solid-state 2H NMR relaxation illuminates functional dynamics of retinal cofactor in membrane activation of rhodopsin [Biophysics and Computational Biology]
Solid-state 2H NMR relaxation illuminates functional dynamics of retinal cofactor in membrane activation of rhodopsin
Struts, A. V., Salgado, G. F. J., Brown, M. F....
Date: 2011-05-17
Rhodopsin is a canonical member of the family of G protein-coupled receptors, which transmit signals across cellular membranes and are linked to many drug interventions in humans. Here we show that solid-state 2H NMR relaxation allows investigation of light-induced changes in local ps–ns time scale motions of retinal bound to rhodopsin. Site-specific 2H labels were introduced into methyl groups of the...
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Solid-state 2H NMR relaxation illuminates functional dynamics of retinal cofactor in membrane activation of rhodopsin.
Solid-state 2H NMR relaxation illuminates functional dynamics of retinal cofactor in membrane activation of rhodopsin.
Solid-state 2H NMR relaxation illuminates functional dynamics of retinal cofactor in membrane activation of rhodopsin.
Proc Natl Acad Sci U S A. 2011 Apr 28;
Authors: Struts AV, Salgado GF, Brown MF
Rhodopsin is a canonical member of the family of G protein-coupled receptors, which transmit signals across cellular membranes and are linked to many drug interventions in humans. Here we show that solid-state (2)H NMR relaxation...
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04-30-2011 12:36 PM
[NMR paper] Deuterium NMR structure of retinal in the ground state of rhodopsin.
Deuterium NMR structure of retinal in the ground state of rhodopsin.
Related Articles Deuterium NMR structure of retinal in the ground state of rhodopsin.
Biochemistry. 2004 Oct 12;43(40):12819-28
Authors: Salgado GF, Struts AV, Tanaka K, Fujioka N, Nakanishi K, Brown MF
The conformation of retinal bound to the G protein-coupled receptor rhodopsin is intimately linked to its photochemistry, which initiates the visual process. Site-directed deuterium ((2)H) NMR spectroscopy was used to investigate the structure of retinal within the binding...
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11-24-2010 10:01 PM
[NMR paper] Refinement of the geometry of the retinal binding pocket in dark-adapted bacteriorhod
Refinement of the geometry of the retinal binding pocket in dark-adapted bacteriorhodopsin by heteronuclear solid-state NMR distance measurements.
Related Articles Refinement of the geometry of the retinal binding pocket in dark-adapted bacteriorhodopsin by heteronuclear solid-state NMR distance measurements.
Biochemistry. 2000 Aug 22;39(33):10066-71
Authors: Helmle M, Patzelt H, Ockenfels A, Gärtner W, Oesterhelt D, Bechinger B
The bacterial proton pump bacteriorhodopsin (BR) is a 26.5 kDa seven-transmembrane helical protein. Several...
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11-19-2010 08:29 PM
[NMR paper] Irreversible conformational change of bacterio-opsin induced by binding of retinal du
Irreversible conformational change of bacterio-opsin induced by binding of retinal during its reconstitution to bacteriorhodopsin, as studied by (13)C NMR.
Related Articles Irreversible conformational change of bacterio-opsin induced by binding of retinal during its reconstitution to bacteriorhodopsin, as studied by (13)C NMR.
J Biochem. 2000 May;127(5):861-9
Authors: Yamaguchi S, Tuzi S, Tanio M, Naito A, Lanyi JK, Needleman R, Saitô H
We compared (13)C NMR spectra of Ala- and Val-labeled bacterio-opsin (bO), produced either by bleaching bR...
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11-18-2010 09:15 PM
[NMR paper] NMR structural studies on antifreeze proteins.
NMR structural studies on antifreeze proteins.
Related Articles NMR structural studies on antifreeze proteins.
Biochem Cell Biol. 1998;76(2-3):284-93
Authors: Sönnichsen FD, Davies PL, Sykes BD
Antifreeze proteins (AFPs) are a structurally diverse class of proteins that bind to ice and inhibit its growth in a noncolligative manner. This adsorption-inhibition mechanism operating at the ice surface results in a lowering of the (nonequilibrium) freezing point below the melting point. A lowering of approximately 1 degree C, which is sufficient to...
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11-17-2010 11:06 PM
[NMR paper] NMR constraints on the location of the retinal chromophore in rhodopsin and bathorhod
NMR constraints on the location of the retinal chromophore in rhodopsin and bathorhodopsin.
Related Articles NMR constraints on the location of the retinal chromophore in rhodopsin and bathorhodopsin.
Biochemistry. 1995 Jan 31;34(4):1425-32
Authors: Han M, Smith SO
Rhodopsin is the photoreceptor in vertebrate rod cells responsible for vision at low light intensities. The photoreactive chromophore in rhodopsin is 11-cis-retinal bound to the protein via a protonated Schiff base with Glu113 as the counterion. We have used the observed 13C NMR...
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08-22-2010 03:41 AM
[NMR paper] Structure determination of the cyclohexene ring of retinal in bacteriorhodopsin by so
Structure determination of the cyclohexene ring of retinal in bacteriorhodopsin by solid-state deuterium NMR.
Related Articles Structure determination of the cyclohexene ring of retinal in bacteriorhodopsin by solid-state deuterium NMR.
Biochemistry. 1992 Oct 27;31(42):10390-9
Authors: Ulrich AS, Heyn MP, Watts A
The orientation and conformation of retinal within bacteriorhodopsin of the purple membrane of Halobacterium halobium was established by solid-state deuterium NMR spectroscopy, through the determination of individual chemical bond...
NMR studies of retinal proteins.
Linear Mode
