is dipolar dephasing one of the contributing mechanisms to T2 or they are different ? Thanks
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NMR Excitation, Dephasing and Spin Echoes
NMR Excitation, Dephasing and Spin Echoes
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NMR Excitation, Dephasing and Spin Echoes
This short animation shows the process of NMR excitation in the laboratory and the rotating frame, as well as the dephasing that occurs from field inhomogeneity and the formation of the Hahn spin echo. Please credit (c)2010 Mark Cohen (mscohen@ucla.edu) during re-use.
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nmrlearner
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01-29-2012 07:45 PM
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...
nmrlearner
Journal club
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09-30-2011 05:59 AM
Frequency-selective heteronuclear dephasing and selective carbonyl labeling to deconvolute crowded spectra of membrane proteins by magic angle spinning NMR.
Frequency-selective heteronuclear dephasing and selective carbonyl labeling to deconvolute crowded spectra of membrane proteins by magic angle spinning NMR.
Frequency-selective heteronuclear dephasing and selective carbonyl labeling to deconvolute crowded spectra of membrane proteins by magic angle spinning NMR.
J Magn Reson. 2011 Mar 17;
Authors: Traaseth NJ, Veglia G
We present a new method that combines carbonyl-selective labeling with frequency-selective heteronuclear recoupling to resolve the spectral overlap of magic angle spinning (MAS) NMR...
nmrlearner
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04-13-2011 11:57 PM
Frequency-Selective Heteronuclear Dephasing and Selective Carbonyl Labeling to Deconvolute Crowded Spectra of Membrane Proteins By Magic Angle Spinning NMR
Frequency-Selective Heteronuclear Dephasing and Selective Carbonyl Labeling to Deconvolute Crowded Spectra of Membrane Proteins By Magic Angle Spinning NMR
Publication year: 2011
Source: Journal of Magnetic Resonance, In Press, Accepted Manuscript, Available online 17 March 2011</br>
Nathaniel J., Traaseth , Gianluigi, Veglia</br>
We present a new method that combines carbonyl-selective labeling with frequency-selective heteronuclear recoupling to resolve the spectral overlap of magic angle spinning (MAS) NMR spectra of membrane proteins in fluid lipid membranes with broad lines and...
nmrlearner
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03-18-2011 06:43 AM
[NMR paper] Transverse dephasing optimized solid-state NMR spectroscopy.
Transverse dephasing optimized solid-state NMR spectroscopy.
Related Articles Transverse dephasing optimized solid-state NMR spectroscopy.
J Am Chem Soc. 2003 Nov 19;125(46):13938-9
Authors: De Paëpe G, Giraud N, Lesage A, Hodgkinson P, Böckmann A, Emsley L
It is shown how coherence lifetimes in solid-state NMR experiments can be controlled. New decoupling schemes are introduced which actively optimize dephasing times, providing increases of up to a factor of 2 with respect to the best existing schemes. The new schemes are implemented in...
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11-24-2010 09:16 PM
[NMR paper] Dipolar Waves as NMR maps of helices in proteins.
Dipolar Waves as NMR maps of helices in proteins.
Related Articles Dipolar Waves as NMR maps of helices in proteins.
J Magn Reson. 2003 Aug;163(2):288-99
Authors: Mesleh MF, Opella SJ
Dipolar Waves describe the periodic variation in the magnitudes of dipolar couplings in the backbone of a protein as a function of residue number. They provide a direct link between experimental measurements of dipolar couplings in aligned samples and the periodicity inherent in regular secondary structure elements. It is possible to identify the residues in a...
nmrlearner
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11-24-2010 09:16 PM
[NMR paper] Dipolar waves as NMR maps of protein structure.
Dipolar waves as NMR maps of protein structure.
Related Articles Dipolar waves as NMR maps of protein structure.
J Am Chem Soc. 2002 Apr 24;124(16):4206-7
Authors: Mesleh MF, Veglia G, DeSilva TM, Marassi FM, Opella SJ
The anisotropy of nuclear spin interactions results in a unique mapping of structure to the resonance frequencies and split tings observed in NMR spectra, however, the determination of molecular structure from experimentally measured spectral parameters is complicated by angular ambiguities resulting from the symmetry properties...
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11-24-2010 08:49 PM
[U. of Ottawa NMR Facility Blog] The Dephasing Power of Pulsed Field Gradients
The Dephasing Power of Pulsed Field Gradients
Pulsed field gradients are used in many modern NMR measurements to select specific coherence pathways and eliminate (or at least minimize) the need for time consuming pulse and receiver phase cycles. The gradients are most often used in conjunction with spin echos such that unwanted coherences can be dephased and the desired coherences can be rephased. They are also used to measure diffusion constants or collect DOSY data. It is instructive to examine the magnetization vectors in the active volume of an NMR tube as a function of the gradient...