Estimating side-chain order in methyl-protonated, perdeuterated proteins via multiple-quantum relaxation violated coherence transfer NMR spectroscopy
Estimating side-chain order in methyl-protonated, perdeuterated proteins via multiple-quantum relaxation violated coherence transfer NMR spectroscopy
Abstract Relaxation violated coherence transfer NMR spectroscopy (Tugarinov et al. in J Am Chem Soc 129:1743â??1750, 2007) is an established experimental tool for quantitative estimation of the amplitudes of side-chain motions in methyl-protonated, highly deuterated proteins. Relaxation violated coherence transfer experiments monitor the build-up of methyl proton multiple-quantum coherences that can be created in magnetically equivalent...
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02-11-2012 10:31 AM
Simultaneous acquisition of 13Cαâ??15N and 1Hâ??15Nâ??15N sequential correlations in proteins: application of dual receivers in 3D HNN
Simultaneous acquisition of 13Cαâ??15N and 1Hâ??15Nâ??15N sequential correlations in proteins: application of dual receivers in 3D HNN
Abstract We describe here, adaptation of the HNN pulse sequence for multiple nuclei detection using two independent receivers by utilizing the detectable 13Cα transverse magnetization which was otherwise dephased out in the conventional HNN experiment. It enables acquisition of 2D 13Cαâ??15N sequential correlations along with the standard 3D 15Nâ??15Nâ??1H correlations, which provides directionality to sequential walk in HNN, on one hand, and enhances...
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12-31-2011 10:40 AM
NMR with Multiple Receivers.
NMR with Multiple Receivers.
NMR with Multiple Receivers.
Top Curr Chem. 2011 Aug 12;
Authors: Kup?e E
Parallel acquisition NMR spectroscopy (PANSY) is used to detect simultaneously signals from up to four nuclear species, such as H-1, H-2, C-13, N-15, F-19 and P-31. The conventional COSY, TOCSY, HSQC, HMQC and HMBC pulse sequences have been adapted for such applications. Routine availability of NMR systems that incorporate multiple receivers has led to development of new types of NMR experiments. One such scheme named PANACEA allows unambiguous...
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08-13-2011 12:57 PM
Very simple combination of TROSY, CRINEPT and multiple quantum coherence for signal enhancement in an HN(CO)CA experiment for large proteins
Very simple combination of TROSY, CRINEPT and multiple quantum coherence for signal enhancement in an HN(CO)CA experiment for large proteins
Publication year: 2011
Source: Journal of Magnetic Resonance, In Press, Accepted Manuscript, Available online 3 February 2011</br>
Monika, Bayrhuber , Roland, Riek</br>
Sensitivity enhancement in liquid state nuclear magnetic resonance (NMR) triple resonance experiments for the sequential assignment of proteins is important for the investigation of large proteins or protein complexes. We present here the 3D TROSY-MQ/CRINEPT-HN(CO)CA which makes...
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02-04-2011 07:03 AM
Detecting the "Afterglow" of (13)C NMR in Proteins Using Multiple Receivers.
Detecting the "Afterglow" of (13)C NMR in Proteins Using Multiple Receivers.
Related Articles Detecting the "Afterglow" of (13)C NMR in Proteins Using Multiple Receivers.
J Am Chem Soc. 2010 Dec 2;
Authors: Kupc?e E, Kay LE, Freeman R
We show that the weak signal that remains after (13)C-detected experiments (the (13)C "afterglow") can still be measured with high sensitivity by proton detection. This is illustrated by the incorporation of two experiments, 2D (HA)CACO and 3D (HA)CA(CO)NNH, into a single pulse sequence that makes use of two receivers...
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12-04-2010 07:24 PM
[NMR paper] Determination of multiple ***φ***-torsion angles in proteins by selective and ext
Determination of multiple ***φ***-torsion angles in proteins by selective and extensive (13)C labeling and two-dimensional solid-state NMR.
Related Articles Determination of multiple ***φ***-torsion angles in proteins by selective and extensive (13)C labeling and two-dimensional solid-state NMR.
J Magn Reson. 1999 Aug;139(2):389-401
Authors: Hong M
We describe an approach to efficiently determine the backbone conformation of solid proteins that utilizes selective and extensive (13)C labeling in conjunction with two-dimensional...
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11-18-2010 08:31 PM
Suite of Six NMR Relaxation Dispersion Experiments to Study Multiple-Site Exchange in Proteins
http://pubs.acs.org/isubscribe/journals/jacsat/127/i44/figures/ja054550en00001.gif
Multiple-Site Exchange in Proteins Studied with a Suite of Six NMR Relaxation Dispersion Experiments: An Application to the Folding of a Fyn SH3 Domain Mutant
Dmitry M. Korzhnev, Philipp Neudecker, Anthony Mittermaier, Vladislav Yu. Orekhov, and Lewis E. Kay*
Contribution from the Departments of Medical Genetics, Biochemistry, and Chemistry, The University of Toronto, Toronto, Ontario M5S 1A8, Canada, and Swedish NMR Center at Göteborg University, Box 465, 405 30 Göteborg, Sweden
J. Am. Chem....
Detecting the “Afterglow” of 13C NMR in Proteins Using Multiple Receivers
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