[NMR paper] 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.
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...
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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The Use of Residual Dipolar Coupling in Studying Proteins by NMR.
The Use of Residual Dipolar Coupling in Studying Proteins by NMR.
The Use of Residual Dipolar Coupling in Studying Proteins by NMR.
Top Curr Chem. 2011 Sep 28;
Authors: Chen K, Tjandra N
Abstract
The development of residual dipolar coupling (RDC) in protein NMR spectroscopy, over a decade ago, has become a useful and almost routine tool for accurate protein solution structure determination. RDCs provide orientation information of magnetic dipole-dipole interaction vectors within a common reference frame. Its measurement requires a...
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09-30-2011 06:00 AM
The Use of Residual Dipolar Coupling in Studying Proteins by NMR.
The Use of Residual Dipolar Coupling in Studying Proteins by NMR.
The Use of Residual Dipolar Coupling in Studying Proteins by NMR.
Top Curr Chem. 2011 Sep 28;
Authors: Chen K, Tjandra N
Abstract
The development of residual dipolar coupling (RDC) in protein NMR spectroscopy, over a decade ago, has become a useful and almost routine tool for accurate protein solution structure determination. RDCs provide orientation information of magnetic dipole-dipole interaction vectors within a common reference frame. Its measurement requires a...
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09-30-2011 05:59 AM
[NMR paper] Studying excited states of proteins by NMR spectroscopy.
Studying excited states of proteins by NMR spectroscopy.
Related Articles Studying excited states of proteins by NMR spectroscopy.
Nat Struct Biol. 2001 Nov;8(11):932-5
Authors: Mulder FA, Mittermaier A, Hon B, Dahlquist FW, Kay LE
Protein structure is inherently dynamic, with function often predicated on excursions from low to higher energy conformations. For example, X-ray studies of a cavity mutant of T4 lysozyme, L99A, show that the cavity is sterically inaccessible to ligand, yet the protein is able to bind substituted benzenes rapidly....
SA’s most powerful microscope: studying subatomic proteins to find cures - San Antonio Report
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