Publication date: 2 February 2018 Source:Biophysical Journal, Volume 114, Issue 3, Supplement 1
Author(s): Xiaolin Xu, Andrey V. Struts, Aswini Kumar Giri, Trivikram R. Molugu, Charitha Guruge, Samira Faylough, Carolina L. Nascimento, Nasri Nesnas, Victor J. Hruby, Michael F. Brown
[NMR paper] Application of Paramagnetic Relaxation Enhancements to Accelerate the Acquisition of 2D and 3D Solid-State NMR Spectra of Oriented Membrane Proteins.
Application of Paramagnetic Relaxation Enhancements to Accelerate the Acquisition of 2D and 3D Solid-State NMR Spectra of Oriented Membrane Proteins.
Related Articles Application of Paramagnetic Relaxation Enhancements to Accelerate the Acquisition of 2D and 3D Solid-State NMR Spectra of Oriented Membrane Proteins.
Methods. 2017 Dec 21;:
Authors: Wang S, Gopinath T, Veglia G
Abstract
Oriented sample solid-state NMR (OS-ssNMR) spectroscopy is uniquely suited to determine membrane protein topology at the atomic resolution in liquid...
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12-25-2017 04:28 PM
Application of Paramagnetic Relaxation Enhancements to Accelerate the Acquisition of 2D and 3D Solid-State NMR Spectra of Oriented Membrane Proteins
Application of Paramagnetic Relaxation Enhancements to Accelerate the Acquisition of 2D and 3D Solid-State NMR Spectra of Oriented Membrane Proteins
Publication date: Available online 22 December 2017
Source:Methods</br>
Author(s): Songlin Wang, T. Gopinath, Gianluigi Veglia</br>
Oriented sample solid-state NMR (OS-ssNMR) spectroscopy is uniquely suited to determine membrane protein topology at the atomic resolution in liquid crystalline bilayers under physiological temperature. However, the inherent low sensitivity of this technique has hindered the throughput...
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12-23-2017 06:08 PM
Dynamics of Methyl Groups in Membrane Proteins Studied by Deterium Solid State NMR Relaxation
Dynamics of Methyl Groups in Membrane Proteins Studied by Deterium Solid State NMR Relaxation
Publication date: 16 February 2016
Source:Biophysical Journal, Volume 110, Issue 3, Supplement 1</br>
Author(s): Xiaolin Xu, Andrey V. Struts, Aswini Kumar Giri, Trivikram R. Molugu, Charitha Guruge, Samira Faylough, Carolina L. Nascimento, Nasri Nesnas, Victor J. Hruby, Michael F. Brown</br>
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02-17-2016 07:50 PM
[NMR paper] Internal protein dynamics on ps to ?s timescales as studied by multi-frequency (15)N solid-state NMR relaxation.
Internal protein dynamics on ps to ?s timescales as studied by multi-frequency (15)N solid-state NMR relaxation.
Related Articles Internal protein dynamics on ps to ?s timescales as studied by multi-frequency (15)N solid-state NMR relaxation.
J Biomol NMR. 2013 Sep 19;
Authors: Zinkevich T, Chevelkov V, Reif B, Saalwächter K, Krushelnitsky A
Abstract
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09-21-2013 06:50 PM
An ensemble dynamics approach to decipher solid-state NMR observables of membrane proteins
An ensemble dynamics approach to decipher solid-state NMR observables of membrane proteins
February 2012
Publication year: 2012
Source:Biochimica et Biophysica Acta (BBA) - Biomembranes, Volume 1818, Issue 2</br>
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Solid-state NMR (SSNMR) is an invaluable tool for determining orientations of membrane proteins and peptides in lipid bilayers. Such orientational descriptions provide essential information about membrane protein functions. However, when a semi-static single conformer model is used to interpret various SSNMR observables, important dynamics information can...
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02-03-2013 10:13 AM
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
Structure and dynamics of cationic membrane peptides and proteins: Insights from solid-state NMR.
Structure and dynamics of cationic membrane peptides and proteins: Insights from solid-state NMR.
Structure and dynamics of cationic membrane peptides and proteins: Insights from solid-state NMR.
Protein Sci. 2011 Feb 22;
Authors: Hong M, Su Y
Many membrane peptides and protein domains contain functionally important cationic Arg and Lys residues, whose insertion into the hydrophobic interior of the lipid bilayer encounters significant energy barriers. To understand how these cationic molecules overcome the free energy barrier to insert into the...
Dynamics of Membrane Proteins Studied by Solid State 2H NMR Relaxation
Linear Mode
