Related ArticlesLongitudinal Relaxation Enhancement in (1) H NMR Spectroscopy of Tissue Metabolites via Spectrally Selective Excitation.
Chemistry. 2013 Sep 3;
Authors: Shemesh N, Dumez JN, Frydman L
Abstract
Nuclear magnetic resonance spectroscopy is governed by longitudinal (T1 ) relaxation. For protein and nucleic acid experiments in solutions, it is well established that apparent T1 values can be enhanced by selective excitation of targeted resonances. The present study explores such longitudinal relaxation enhancement (LRE) effects for molecules residing in biological tissues. The longitudinal relaxation recovery of tissue resonances positioned both down- and upfield of the water peak were measured by spectrally selective excitation/refocusing pulses, and compared with conventional water-suppressed, broadband-excited counterparts at 9.4 T. Marked LRE effects with up to threefold reductions in apparent T1 values were observed as expected for resonances in the 6-9 ppm region; remarkably, statistically significant LRE effects were also found for several non-exchanging metabolite resonances in the 1-4 ppm region, encompassing 30-50 % decreases in apparent T1 values. These LRE effects suggest a novel means of increasing the sensitivity of tissue-oriented experiments, and open new vistas to investigate the nature of interactions among metabolites, water and macromolecules at a molecular level.
PMID: 24038462 [PubMed - as supplied by publisher]
[Question from NMRWiki Q&A forum] 1D NOESY with selective excitation and water suppression
1D NOESY with selective excitation and water suppression
Hi,
I am trying to collect 1D NOESY spectrum of a small protein in 90% H2O with selective excitation so I could follow a few NOEs without running a whole 2D experiment. Is there any sequence in Varian BioPack that I could use for that? I cannot achieve water suppression with the standard 'Noesy1D' sequence and all the other seem to not allow to selectively irradiate only one peak. Maybe it is just a matter of right parameters but I don't know how to set them properly - if so I will appreciate any advice.
Thanks
nmrlearner
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09-11-2013 09:15 PM
13C relaxation experiments for aromatic side chains employing longitudinal- and transverse-relaxation optimized NMR spectroscopy
13C relaxation experiments for aromatic side chains employing longitudinal- and transverse-relaxation optimized NMR spectroscopy
Abstract Aromatic side chains are prevalent in protein binding sites, perform functional roles in enzymatic catalysis, and form an integral part of the hydrophobic core of proteins. Thus, it is of great interest to probe the conformational dynamics of aromatic side chains and its response to biologically relevant events. Indeed, measurements of 13C relaxation rates in aromatic moieties have a long history in biomolecular NMR, primarily in the context of...
nmrlearner
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07-05-2012 04:13 AM
Elucidating slow binding kinetics of a protein without observable bound resonances by longitudinal relaxation NMR spectroscopy
Elucidating slow binding kinetics of a protein without observable bound resonances by longitudinal relaxation NMR spectroscopy
Abstract We developed a new method to elucidate the binding kinetics kon and koff, and the dissociation constant KD (=koff/kon), of protein-protein interactions without observable bound resonances of the protein of interest due to high molecular weight in a complex with a large target protein. In our method, kon and koff rates are calculated from the analysis of longitudinal relaxation rates of free resonances measured for multiple samples containing different...
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06-06-2011 12:53 AM
Elucidating slow binding kinetics of a protein without observable bound resonances by longitudinal relaxation NMR spectroscopy.
Elucidating slow binding kinetics of a protein without observable bound resonances by longitudinal relaxation NMR spectroscopy.
Elucidating slow binding kinetics of a protein without observable bound resonances by longitudinal relaxation NMR spectroscopy.
J Biomol NMR. 2011 May 28;
Authors: Sugase K
We developed a new method to elucidate the binding kinetics k(on) and k(off), and the dissociation constant K(D) (=k(off)/k(on)), of protein-protein interactions without observable bound resonances of the protein of interest due to high molecular...
nmrlearner
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06-01-2011 02:30 PM
[NMR paper] Longitudinal (1)H relaxation optimization in TROSY NMR spectroscopy.
Longitudinal (1)H relaxation optimization in TROSY NMR spectroscopy.
Related Articles Longitudinal (1)H relaxation optimization in TROSY NMR spectroscopy.
J Am Chem Soc. 2002 Oct 30;124(43):12898-902
Authors: Pervushin K, Vögeli B, Eletsky A
A general method to enhance the sensitivity of the multidimensional NMR experiments performed at high-polarizing magnetic field via the significant reduction of the longitudinal proton relaxation times is described. The method is based on the use of two vast pools of "thermal bath" 1H spins residing on...
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11-24-2010 08:58 PM
[NMR paper] Highly selective excitation in biomolecular NMR by frequency-switched single-transiti
Highly selective excitation in biomolecular NMR by frequency-switched single-transition cross-polarization.
Related Articles Highly selective excitation in biomolecular NMR by frequency-switched single-transition cross-polarization.
J Am Chem Soc. 2002 Mar 13;124(10):2076-7
Authors: Ferrage F, Eykyn TR, Bodenhausen G
A new method for selective excitation in biomolecular NMR uses two-fold single-transition cross-polarization between protons and nitrogen-15 or carbon-13 nuclei. Switching the frequencies between the forward and backward transfer...
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11-24-2010 08:49 PM
A Selective NMR Method for Detecting Choline Containing Compounds in Liver Tissue: Th
A Selective NMR Method for Detecting Choline Containing Compounds in Liver Tissue: The 1H-14N HSQC Experiment
Jiezhen Mao, Ling Jiang, Bin Jiang, Maili Liu and Xi-an Mao
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja107745g/aop/images/medium/ja-2010-07745g_0003.gif
Journal of the American Chemical Society
DOI: 10.1021/ja107745g
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/3IJa7rhbOjw
nmrlearner
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11-20-2010 06:29 AM
[U. of Ottawa NMR Facility Blog] Gradient Spin Echoes for Selective Excitation
Gradient Spin Echoes for Selective Excitation
Shaped excitation pulses can replace the non-selective hard pulses typically used in a one-pulse measurement to achieve selective excitation. Another method of achieving selective excitation is the gradient spin echo using a selective 180° pulse. This technique is demonstrated in the figure below. http://4.bp.blogspot.com/_5wBTR2kKTqA/S_UxeG5oXdI/AAAAAAAAAzc/BHWef-Tse7s/s400/grad_spin_echo.jpgA non-selective hard 90°x pulse is first given followed by a pair of identical pulsed field gradients sandwiching a soft selective 180° pulse about the y...
Longitudinal Relaxation Enhancement in (1) H NMR Spectroscopy of Tissue Metabolites via Spectrally Selective Excitation.
Linear Mode
