Abstract Experimental sensitivity remains a major drawback for the application of NMR spectroscopy to fragile and low concentrated biomolecular samples. Here we describe an efficient polarization enhancement mechanism in longitudinal-relaxation enhanced fast-pulsing triple-resonance experiments. By recovering undetectable 1H polarization originating from longitudinal relaxation during the pulse sequence, the steady-state 15N polarization becomes enhanced by up to a factor of ~5 with respect to thermal equilibrium yielding significant sensitivity improvements compared to conventional schemes. The benefits of BEST-TROSY experiments at high magnetic field strength are illustrated for various protein applications, but they will be equally useful for other protonated macromolecular systems.
Content Type Journal Article
DOI 10.1007/s10858-010-9461-5
Authors
Adrien Favier, IBS, Institut de Biologie Structurale Jean-Pierre Ebel, 41 rue Jules Horowitz, 38027 Grenoble, France
Bernhard Brutscher, IBS, Institut de Biologie Structurale Jean-Pierre Ebel, 41 rue Jules Horowitz, 38027 Grenoble, France
Repetitive cross-polarization contacts via equilibration-re-equilibration of the proton bath: sensitivity enhancement for NMR of membrane proteins reconstituted in magnetically aligned bicelles
Repetitive cross-polarization contacts via equilibration-re-equilibration of the proton bath: sensitivity enhancement for NMR of membrane proteins reconstituted in magnetically aligned bicelles
Publication year: 2011
Source: Journal of Magnetic Resonance, In Press, Accepted Manuscript, Available online 2 July 2011</br>
Wenxing, Tang , Alexander A., Nevzorov</br>
Thermodynamic limit of magnetization corresponding to the intact proton bath often cannot be transferred in a single cross-polarization contact. This is mainly due to the finite ratio between the number densities of the high-...
Straightforward, effective calibration of SPINAL-64 decoupling results in the enhancement of sensitivity and resolution of biomolecular solid-state NMR.
Straightforward, effective calibration of SPINAL-64 decoupling results in the enhancement of sensitivity and resolution of biomolecular solid-state NMR.
Straightforward, effective calibration of SPINAL-64 decoupling results in the enhancement of sensitivity and resolution of biomolecular solid-state NMR.
J Magn Reson. 2010 Dec 31;
Authors: Comellas G, Lopez JJ, Nieuwkoop AJ, Lemkau LR, Rienstra CM
We describe a simple yet highly effective optimization strategy for SPINAL-64 (1)H decoupling conditions for magic-angle spinning solid-state NMR. With...
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02-08-2011 06:28 PM
Overcoming the solubility limit with solubility-enhancement tags: successful applications in biomolecular NMR studies
Overcoming the solubility limit with solubility-enhancement tags: successful applications in biomolecular NMR studies
Abstract Although the rapid progress of NMR technology has significantly expanded the range of NMR-trackable systems, preparation of NMR-suitable samples that are highly soluble and stable remains a bottleneck for studies of many biological systems. The application of solubility-enhancement tags (SETs) has been highly effective in overcoming solubility and sample stability issues and has enabled structural studies of important biological systems previously deemed...
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01-09-2011 12:46 PM
Straightforward, effective calibration of SPINAL-64 decoupling results in the enhancement of sensitivity and resolution of biomolecular solid-state NMR
Straightforward, effective calibration of SPINAL-64 decoupling results in the enhancement of sensitivity and resolution of biomolecular solid-state NMR
Publication year: 2010
Source: Journal of Magnetic Resonance, In Press, Accepted Manuscript, Available online 31 December 2010</br>
Gemma, Comellas , Jakob J., Lopez , Andrew J., Nieuwkoop , Luisel R., Lemkau , Chad M., Rienstra</br>
We describe a simple yet highly effective optimization strategy for SPINAL-64 1H decoupling conditions for magic-angle spinning solid-state NMR. With adjustment of the phase angles in a coupled manner,...
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01-01-2011 08:57 AM
Recovering lost magnetization: polarization enhancement in biomolecular NMR.
Recovering lost magnetization: polarization enhancement in biomolecular NMR.
Recovering lost magnetization: polarization enhancement in biomolecular NMR.
J Biomol NMR. 2010 Dec 30;
Authors: Favier A, Brutscher B
Experimental sensitivity remains a major drawback for the application of NMR spectroscopy to fragile and low concentrated biomolecular samples. Here we describe an efficient polarization enhancement mechanism in longitudinal-relaxation enhanced fast-pulsing triple-resonance experiments. By recovering undetectable (1)H polarization...
Recovering lost magnetization: polarization enhancement in biomolecular NMR
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