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 with selectively labeled retinal provide information on structural changes of the chromophore in different protein states. Moreover (2)H NMR relaxation time measurements allow one to study the dynamics of the ligand during the transition from the inactive to the active state. Here we describe the methodological aspects of solid-state (2)H NMR spectroscopy for functional studies of rhodopsin, with an emphasis on the dynamics of the retinal cofactor. We provide complete protocols for the preparation of NMR samples of rhodopsin with 11-cis-retinal selectively deuterated at the methyl groups in aligned membranes. In addition we review optimized conditions for trapping the rhodopsin photointermediates; and we address the challenging problem of trapping the signaling state of rhodopsin in aligned membrane films.
[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...
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12-27-2014 03:04 AM
A Studyof Phenylalanine Side-Chain Dynamics in Surface-AdsorbedPeptides Using Solid-State Deuterium NMR and Rotamer Library Statistics
A Studyof Phenylalanine Side-Chain Dynamics in Surface-AdsorbedPeptides Using Solid-State Deuterium NMR and Rotamer Library Statistics
Kun Li, Prashant S. Emani, Jason Ash, Michael Groves and Gary P. Drobny
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja504677d/aop/images/medium/ja-2014-04677d_0008.gif
Journal of the American Chemical Society
DOI: 10.1021/ja504677d
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/d2WMAZNh-I4
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08-06-2014 07:59 AM
[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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01-29-2014 02:01 PM
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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05-17-2011 08:40 PM
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] Investigation of the dynamics of an elastin-mimetic polypeptide using solid-state NMR
Investigation of the dynamics of an elastin-mimetic polypeptide using solid-state NMR.
Related Articles Investigation of the dynamics of an elastin-mimetic polypeptide using solid-state NMR.
Magn Reson Chem. 2004 Feb;42(2):267-75
Authors: Yao XL, Conticello VP, Hong M
Elastin is the main structural protein that provides elasticity to various tissues and organs in vertebrates. Molecular motions are believed to play a significant role in its elasticity. We have used solid-state NMR spectroscopy to characterize the dynamics of an elastin-mimetic...
Investigation of rhodopsin dynamics in its signaling state by solid-state deuterium NMR spectroscopy.
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