Water proton NMR-a sensitive probe for solute association.
Chem Commun (Camb). 2015 Mar 19;
Authors: Feng Y, Taraban MB, Yu YB
Abstract
It is found that the transverse relaxation rate R2 of the water protons can be used to quantify protein aggregation and surfactant micellization in water. The simplicity and high intensity of the water proton signal enables non-invasive chemical analysis not readily achievable through solute proton signals, such as inspecting finished biologic products.
PMID: 25788228 [PubMed - as supplied by publisher]
A pH-Sensitive, Colorful,Lanthanide-Chelating ParamagneticNMR Probe
A pH-Sensitive, Colorful,Lanthanide-Chelating ParamagneticNMR Probe
Wei-Min Liu, Peter H. J. Keizers, Mathias A. S. Hass, Anneloes Blok, Monika Timmer, Alexi J. C. Sarris, Mark Overhand and Marcellus Ubbink
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja307824e/aop/images/medium/ja-2012-07824e_0011.gif
Journal of the American Chemical Society
DOI: 10.1021/ja307824e
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/NuKda-fEQQ4
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10-10-2012 03:14 PM
NMR Detection of pH-Dependent Histidine–Water Proton Exchange Reveals the Conduction Mechanism of a Transmembrane Proton Channel
NMR Detection of pH-Dependent Histidine–Water Proton Exchange Reveals the Conduction Mechanism of a Transmembrane Proton Channel
Fanghao Hu, Klaus Schmidt-Rohr and Mei Hong
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja2081185/aop/images/medium/ja-2011-081185_0008.gif
Journal of the American Chemical Society
DOI: 10.1021/ja2081185
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/C3pPoB5_PR8
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10-22-2011 10:16 AM
[Question from NMRWiki Q&A forum] Tuning probe failed after a dual probe was replaced with a BBI probe
Tuning probe failed after a dual probe was replaced with a BBI probe
We generally use Dual to run 13C and BBI to run 2D. After changed the probe, the command "edhead" was used to set the probe. Put the sample tube, lock the solvent, and then type "atma" to tune the probe. We always do it like this, but now we can not tune the proton after installed the BBI probe (13C is OK). The dip can not be found by "atma", and "atmm" was also not work on forming a dip. What is the most possible reason for this error? How to solve it and avoid it in the future ? Thanks. (Instrument: Bruker 400 MHz,...
Slight mistuning of a cryogenic probe significantly perturbs the water 1H precession frequency
Slight mistuning of a cryogenic probe significantly perturbs the water 1H precession frequency
Abstract A shift of the water proton precession frequency is described that can introduce errors in chemical shifts derived using the water signal as the chemical shift reference. This shift, fs, arises as a consequence of radiation damping when the water proton and detector circuit resonance frequencies differ. Herein it is shown that experimental values of fs, measured as a function of detector circuit tuning offset for 500 and 900 MHz cryogenic probes, are in good agreement with theory. Of...
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01-09-2011 12:46 PM
[NMR paper] Proton NMR visible mobile lipid signals in sensitive and multidrug-resistant K562 cel
Proton NMR visible mobile lipid signals in sensitive and multidrug-resistant K562 cells are modulated by rafts.
Related Articles Proton NMR visible mobile lipid signals in sensitive and multidrug-resistant K562 cells are modulated by rafts.
Cancer Cell Int. 2005 Feb 9;5(1):2
Authors: Mannechez A, Reungpatthanaphong P, de Certaines JD, Leray G, Le Moyec L
BACKGROUND: Most cancer cells are characterized by mobile lipids visible on proton NMR (1H-NMR), these being comprised mainly of methyl and methylene signals from lipid acyl chains....
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11-24-2010 11:14 PM
[NMR paper] Nature of lysozyme-water interactions by proton NMR.
Nature of lysozyme-water interactions by proton NMR.
Related Articles Nature of lysozyme-water interactions by proton NMR.
Biochem Cell Biol. 1991 May-Jun;69(5-6):341-5
Authors: Prosser S, Peemoeller H
Proton spin-lattice relaxation measurements were performed in 10 mM lysozyme solution as a function of temperature and degree of substitution of solvent H2O with D2O. The results show that in the temperature range from 274 to 323 K, the intermolecular lysozyme proton water proton coupling contributes appreciably to the observed water proton...