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 in both medicine and chemistry. L: -carnitine (3-hydroxy-4-N-trimethylammonium butyrate) is an important metabolite which participates in a series of biological paths and therefore its determination is of diagnostic importance. A single quantum coherence filtering (1)H NMR methodology was used for the accurate and rapid determination of L: -carnitine in human serum samples. The methodology is based on spectral simplification, and specifically on the distinction of the N-methyl proton signal of L: -carnitine that is greatly overlapped in the (1)H-NMR spectrum of serum. The quantitative results provided by the proposed method are in excellent agreement with those obtained by the enzymatic method, which is widely used. The proposed method is rapid (~20*min of experimental time), selective, sensitive, and has good analytical characteristics (accuracy, reproducibility). Selected protein precipitation methods were also investigated and sample pretreatment with EtOH is suggested.
PMID: 21221550 [PubMed - as supplied by publisher]
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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(1)H assisted (13)C/(15)N heteronuclear correlation spectroscopy in oriented sample solid-state NMR of single crystal and magnetically aligned samples.
(1)H assisted (13)C/(15)N heteronuclear correlation spectroscopy in oriented sample solid-state NMR of single crystal and magnetically aligned samples.
(1)H assisted (13)C/(15)N heteronuclear correlation spectroscopy in oriented sample solid-state NMR of single crystal and magnetically aligned samples.
J Magn Reson. 2011 Apr 9;
Authors: Lin EC, Opella SJ
(1)H-irradiation under mismatched Hartmann-Hahn conditions provides an alternative mechanism for carrying out (15)N/(13)C transfers in triple-resonance heteronuclear correlation spectroscopy...
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1H Assisted 13C/15N Heteronuclear Correlation Spectroscopy in Oriented Sample Solid-State NMR of Single Crystal and Magnetically Aligned Samples
1H Assisted 13C/15N Heteronuclear Correlation Spectroscopy in Oriented Sample Solid-State NMR of Single Crystal and Magnetically Aligned Samples
Publication year: 2011
Source: Journal of Magnetic Resonance, In Press, Accepted Manuscript, Available online 9 April 2011</br>
Eugene C., Lin , Stanley J., Opella</br>
1H-irradiation under mismatched Hartmann-Hahn conditions provides an alternative mechanism for carrying out 15N/13C transfers in triple-resonance heteronuclear correlation spectroscopy (HETCOR) on stationary samples of single crystals and aligned samples of biopolymers, which...
[NMR paper] Removal of zero-quantum coherence in protein NMR spectra using SESAM decoupling and s
Removal of zero-quantum coherence in protein NMR spectra using SESAM decoupling and suppression of decoupling sidebands.
Related Articles Removal of zero-quantum coherence in protein NMR spectra using SESAM decoupling and suppression of decoupling sidebands.
J Magn Reson B. 1996 Feb;110(2):219-24
Authors: Weigelt J, Hammarstroem A, Bermel W, Otting G
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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...