Related ArticlesColor-discriminating retinal configurations of sensory rhodopsin I by photo-irradiation solid-state NMR spectroscopy.
Angew Chem Int Ed Engl. 2014 Jul 1;53(27):6960-4
Authors: Yomoda H, Makino Y, Tomonaga Y, Hidaka T, Kawamura I, Okitsu T, Wada A, Sudo Y, Naito A
Abstract
SRI (sensory rhodopsin I) can discriminate multiple colors for the attractant and repellent phototaxis. Studies aimed at revealing the color-dependent mechanism show that SRI is a challenging system not only in photobiology but also in photochemistry. During the photoreaction of SRI, an M-intermediate (attractant) transforms into a P-intermediate (repellent) by absorbing blue light. Consequently, SRI then cycles back to the G-state. The photoreactions were monitored with the (13)C NMR signals of [20-(13)C]retnal-SrSRI using in situ photo-irradiation solid-state NMR spectroscopy. The M-intermediate was trapped at -40 °C by illumination at 520 nm. It was transformed into the P-intermediate by subsequent illumination at 365 nm. These results reveal that the G-state could be directly transformed to the P-intermediate by illumination at 365 nm. Thus, the stationary trapped M- and P-intermediates are responsible for positive and negative phototaxis, respectively.
[NMR paper] Investigation of rhodopsin dynamics in its signaling state by solid-state deuterium NMR spectroscopy.
Investigation of rhodopsin dynamics in its signaling state by solid-state deuterium NMR spectroscopy.
Investigation of rhodopsin dynamics in its signaling state by solid-state deuterium NMR spectroscopy.
Methods Mol Biol. 2015;1271:133-58
Authors: Struts AV, Chawla U, Perera SM, Brown MF
Abstract
Site-directed deuterium NMR spectroscopy is a valuable tool to study the structural dynamics of biomolecules in cases where solution NMR is inapplicable. Solid-state (2)H NMR spectral studies of aligned membrane samples of rhodopsin...
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[NMR paper] Advanced solid-state NMR techniques for characterization of membrane protein structure and dynamics: Application to Anabaena Sensory Rhodopsin.
Advanced solid-state NMR techniques for characterization of membrane protein structure and dynamics: Application to Anabaena Sensory Rhodopsin.
Related Articles Advanced solid-state NMR techniques for characterization of membrane protein structure and dynamics: Application to Anabaena Sensory Rhodopsin.
J Magn Reson. 2014 Dec 26;
Authors: Ward ME, Brown LS, Ladizhansky V
Abstract
Studies of the structure, dynamics, and function of membrane proteins (MPs) have long been considered one of the main applications of solid-state...
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[NMR paper] Advanced Solid-State NMR Techniques for Characterization of Membrane Protein Structure and Dynamics: Application to Anabaena Sensory Rhodopsin
Advanced Solid-State NMR Techniques for Characterization of Membrane Protein Structure and Dynamics: Application to Anabaena Sensory Rhodopsin
Publication date: Available online 26 December 2014
Source:Journal of Magnetic Resonance</br>
Author(s): Meaghan E. Ward , Leonid S. Brown , Vladimir Ladizhansky</br>
Studies of the structure, dynamics, and function of membrane proteins (MPs) have long been considered one of the main applications of solid-state NMR (SSNMR). Advances in instrumentation, and the plethora of new SSNMR methodologies developed over the past...
[NMR paper] Conformational dynamics of a seven transmembrane helical protein Anabaena Sensory Rhodopsin probed by solid-state NMR.
Conformational dynamics of a seven transmembrane helical protein Anabaena Sensory Rhodopsin probed by solid-state NMR.
Related Articles Conformational dynamics of a seven transmembrane helical protein Anabaena Sensory Rhodopsin probed by solid-state NMR.
J Am Chem Soc. 2014 Jan 27;
Authors: Good DB, Wang S, Ward ME, Struppe JO, Brown LS, Lewandowski JR, Ladizhansky V
Abstract
The ability to detect and characterize molecular motions represents one of the unique strengths of Nuclear Magnetic Resonance (NMR) spectroscopy. In this study we...
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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...