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
Origin and removal of mixed-phase artifacts in gradient sensitivity enhanced heteronuclear single quantum correlation spectra
Origin and removal of mixed-phase artifacts in gradient sensitivity enhanced heteronuclear single quantum correlation spectra
Abstract Here we describe phasing anomalies observed in gradient sensitivity enhanced 15N-1H HSQC spectra, and analyze their origin. It is shown that, as a result of 15N off-resonance effects, dispersive contributions to the 1H signal become detectable, and lead to 15N-offset dependent phase errors. Strategies that effectively suppress these artifacts are presented.
Content Type Journal Article
Category Article
Pages 199-207
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09-30-2011 08:01 PM
[Question from NMRWiki Q&A forum] adiabatic decoupling
adiabatic decoupling
Hi NMRwikiers, for measuring scalar couplings we use some HSQC pulse sequences modified for obtaining the coupling in F1-dimension as a splitting of doublets for CH2 groups. As high resolution is needed we use high folding in the acqusition, but as a result we obtain a lot of coupling artifacts in phenyl signals. We think that the use of adiabatic decoupling schemes should give a reasonably good spectrum of phenyls but I have no experience in adiabatic decoupling. Anyone can give me a hand for Bruker spectrometers?
Check if somebody has answered this question on...
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05-24-2011 10:02 PM
Singular spectrum analysis for an automated solvent artifact removal and baseline correction of 1D NMR spectra.
Singular spectrum analysis for an automated solvent artifact removal and baseline correction of 1D NMR spectra.
Singular spectrum analysis for an automated solvent artifact removal and baseline correction of 1D NMR spectra.
J Magn Reson. 2011 Mar 6;
Authors: De Sanctis S, Malloni WM, Kremer W, Tomé AM, Lang EW, Neidig KP, Kalbitzer HR
NMR spectroscopy in biology and medicine is generally performed in aqueous solutions, thus in (1)H NMR spectroscopy, the dominant signal often stems from the partly suppressed solvent and can be many orders of...
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04-05-2011 10:22 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
A new method for the determination of free L: -carnitine in serum samples based on high field single quantum coherence filtering (1)H-NMR spectroscopy.
A new method for the determination of free L: -carnitine in serum samples based on high field single quantum coherence filtering (1)H-NMR spectroscopy.
A new method for the determination of free L: -carnitine in serum samples based on high field single quantum coherence filtering (1)H-NMR spectroscopy.
Anal Bioanal Chem. 2011 Jan 11;
Authors: Tsiafoulis CG, Exarchou V, Tziova PP, Bairaktari E, Gerothanassis IP, Troganis AN
The rapid and accurate determination of specific metabolites present in biofluids is a very demanding task which is essential...
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01-12-2011 11:11 AM
[Question from NMRWiki Q&A forum] How does removal and re-installation of probe affect shims?
How does removal and re-installation of probe affect shims?
If you remove and later (not too much later) reinstall the probe and you are confident that probe position inside the magnet does not change at all - would you expect the shim set to change?
Do eddy currents due to probe movement affect field homogeneity?
Thanks.
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08-22-2010 02:30 AM
Double quantum filtering homonuclear MAS NMR correlation spectra: a tool for membrane protein studies
Double quantum filtering homonuclear MAS NMR correlation spectra: a tool for membrane protein studies
Jakob J. Lopez, Christoph Kaiser, Sarika Shastri and Clemens Glaubitz
Journal of Biomolecular NMR; 2008; 41(2) pp 97 - 104
Abstract:
13C homonuclear correlation spectra based on proton driven spin diffusion (PDSD) are becoming increasingly important for obtaining distance constraints from multiply labeled biomolecules by MAS NMR. One particular challenging situation arises when such constraints are to be obtained from spectra with a large natural abundance signal background which...