1H magic-angle spinning NMR evolves as a powerful new tool for membrane proteins.
J Magn Reson. 2018 Feb;287:140-152
Authors: Schubeis T, Le Marchand T, Andreas LB, Pintacuda G
Abstract
Building on a decade of continuous advances of the community, the recent development of very fast (60 kHz and above) magic-angle spinning (MAS) probes has revolutionised the field of solid-state NMR. This new spinning regime reduces the 1H-1H dipolar couplings, so that direct detection of the larger magnetic moment available from 1H is now possible at high resolution, not only in deuterated molecules but also in fully-protonated substrates. Such capabilities allow rapid "fingerprinting" of samples with a ten-fold reduction of the required sample amounts with respect to conventional approaches, and permit extensive, robust and expeditious assignment of small-to-medium sized proteins (up to ca. 300 residues), and the determination of inter-nuclear proximities, relative orientations of secondary structural elements, protein-cofactor interactions, local and global dynamics. Fast MAS and 1H detection techniques have nowadays been shown to be applicable to membrane-bound systems. This paper reviews the strategies underlying this recent leap forward in sensitivity and resolution, describing its potential for the detailed characterization of membrane proteins.
1H magic-angle spinning NMR evolves as a powerful new tool for membrane proteins
1H magic-angle spinning NMR evolves as a powerful new tool for membrane proteins
Publication date: February 2018
Source:Journal of Magnetic Resonance, Volume 287</br>
Author(s): Tobias Schubeis, Tanguy Le Marchand, Loren B. Andreas, Guido Pintacuda</br>
Building on a decade of continuous advances of the community, the recent development of very fast (60 kHz and above) magic-angle spinning (MAS) probes has revolutionised the field of solid-state NMR. This new spinning regime reduces the 1H-1H dipolar couplings, so that direct detection of the larger magnetic...
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02-06-2018 07:07 AM
[NMR paper] Magic-Angle-Spinning Solid-State NMR of Membrane Proteins.
Magic-Angle-Spinning Solid-State NMR of Membrane Proteins.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Magic-Angle-Spinning Solid-State NMR of Membrane Proteins.
Methods Enzymol. 2015;557:307-328
Authors: Baker LA, Folkers GE, Sinnige T, Houben K, Kaplan M, van der Cruijsen EA, Baldus M
Abstract
Solid-state NMR spectroscopy (ssNMR) provides increasing possibilities to examine membrane proteins in different molecular settings, ranging...
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05-08-2015 09:18 PM
[NMR paper] Recent advances in magic angle spinning solid state NMR of membrane proteins.
Recent advances in magic angle spinning solid state NMR of membrane proteins.
Recent advances in magic angle spinning solid state NMR of membrane proteins.
Prog Nucl Magn Reson Spectrosc. 2014 Oct;82C:1-26
Authors: Wang S, Ladizhansky V
Abstract
Membrane proteins mediate many critical functions in cells. Determining their three-dimensional structures in the native lipid environment has been one of the main objectives in structural biology. There are two major NMR methodologies that allow this objective to be accomplished....
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Recent advances in magic angle spinning solid state NMR of membrane proteins
From The DNP-NMR Blog:
Recent advances in magic angle spinning solid state NMR of membrane proteins
Wang, S. and V. Ladizhansky, Recent advances in magic angle spinning solid state NMR of membrane proteins. Prog. NMR. Spec., 2014. 82(0): p. 1-26.
http://www.sciencedirect.com/science/article/pii/S0079656514000478
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Recent advances in magic angle spinning solid state NMR of membrane proteins
Recent advances in magic angle spinning solid state NMR of membrane proteins
Publication date: Available online 26 July 2014
Source:Progress in Nuclear Magnetic Resonance Spectroscopy</br>
Author(s): Shenlin Wang , Vladimir Ladizhansky</br>
Membrane proteins mediate many critical functions in cells. Determining their three-dimensional structures in the native lipid environment has been one of the main objectives in structural biology. There are two major NMR methodologies that allow this objective to be accomplished. Oriented sample NMR, which can be applied to...
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07-27-2014 01:05 AM
[NMR paper] High-resolution paramagnetically enhanced solid-state NMR spectroscopy of membrane proteins at fast magic angle spinning.
High-resolution paramagnetically enhanced solid-state NMR spectroscopy of membrane proteins at fast magic angle spinning.
Related Articles High-resolution paramagnetically enhanced solid-state NMR spectroscopy of membrane proteins at fast magic angle spinning.
J Biomol NMR. 2013 Dec 13;
Authors: Ward ME, Wang S, Krishnamurthy S, Hutchins H, Fey M, Brown LS, Ladizhansky V
Abstract
Magic angle spinning nuclear magnetic resonance (MAS NMR) is well suited for the study of membrane proteins in membrane mimetic and native membrane...
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12-18-2013 04:00 PM
[NMR paper] Lipid bilayer preparations of membrane proteins for oriented and magic-angle spinning solid-state NMR samples.
Lipid bilayer preparations of membrane proteins for oriented and magic-angle spinning solid-state NMR samples.
Related Articles Lipid bilayer preparations of membrane proteins for oriented and magic-angle spinning solid-state NMR samples.
Nat Protoc. 2013 Nov;8(11):2256-70
Authors: Das N, Murray DT, Cross TA
Abstract
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Solid-state magic-angle spinning NMR of membrane proteins and protein–ligand interactions
Solid-state magic-angle spinning NMR of membrane proteins and protein–ligand interactions
April 2012
Publication year: 2012
Source:European Journal of Cell Biology, Volume 91, Issue 4</br>
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Structural biology is developing into a universal tool for visualizing biological processes in space and time at atomic resolution. The field has been built by established methodology like X-ray crystallography, electron microscopy and solution NMR and is now incorporating new techniques, such as small-angle X-ray scattering, electron tomography, magic-angle-spinning solid-state...