Signal amplification by reversible exchange (SABRE) can enhance nuclear magnetic resonance signals by several orders of magnitude. However, until now this was limited to a small number of model target molecules. Here, a new convenient method for SABRE activation applicable to a variety of synthetic model oligopeptides is demonstrated. For the first time, a highly SABRE-active pyridine-based biocompatible molecular framework is incorporated into synthetic oligopeptides. The SABRE activity is preserved, demonstrating the importance of such earmarking. Finally, a crucial exchange process responsible for SABRE activity is identified and discussed.
Effective PHIP labeling of bioactive peptides boosts the intensity of the NMR signal
From The DNP-NMR Blog:
Effective PHIP labeling of bioactive peptides boosts the intensity of the NMR signal
Sauer, G., et al., Effective PHIP labeling of bioactive peptides boosts the intensity of the NMR signal. Angew Chem Int Ed Engl, 2014. 53(47): p. 12941-5.
http://www.ncbi.nlm.nih.gov/pubmed/25296746
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03-04-2015 08:57 PM
The Feasibility of Formation and Kinetics of NMR Signal Amplification by Reversible Exchange (SABRE) at High Magnetic Field (9.4 T)
From The DNP-NMR Blog:
The Feasibility of Formation and Kinetics of NMR Signal Amplification by Reversible Exchange (SABRE) at High Magnetic Field (9.4 T)
Barskiy, D.A., et al., The feasibility of formation and kinetics of NMR signal amplification by reversible exchange (SABRE) at high magnetic field (9.4 T). J Am Chem Soc, 2014. 136(9): p. 3322-5.
http://www.ncbi.nlm.nih.gov/pubmed/24528143
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05-19-2014 09:25 PM
DNP by Thermal Mixing under Optimized Conditions Yields >60 000-fold Enhancement of 89Y NMR Signal
DNP by Thermal Mixing under Optimized Conditions Yields >60 000-fold Enhancement of 89Y NMR Signal
Lloyd Lumata, Ashish K. Jindal, Matthew E. Merritt, Craig R. Malloy, A. Dean Sherry and Zoltan Kovacs
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja201880y/aop/images/medium/ja-2011-01880y_0010.gif
Journal of the American Chemical Society
DOI: 10.1021/ja201880y
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/lZjUD7bs_fI
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05-13-2011 07:49 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.
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
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
Signal enhancement in protein NMR using the spin-noise tuning optimum
Signal enhancement in protein NMR using the spin-noise tuning optimum
Abstract We have assessed the potential of an alternative probe tuning strategy based on the spin-noise response for application in common high-resolution multi-dimensional biomolecular NMR experiments with water signal suppression on aqueous and salty samples. The method requires the adjustment of the optimal tuning condition, which may be offset by several 100 kHz from the conventional tuning settings using the noise response of the water protons as an indicator. Although the radio frequency-pulse durations are...
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10-09-2010 03:03 AM
Signal enhancement in protein NMR using the spin-noise tuning optimum.
Signal enhancement in protein NMR using the spin-noise tuning optimum.
Signal enhancement in protein NMR using the spin-noise tuning optimum.
J Biomol NMR. 2010 Oct 6;
Authors: Nausner M, Goger M, Bendet-Taicher E, Schlagnitweit J, Jerschow A, Müller N
We have assessed the potential of an alternative probe tuning strategy based on the spin-noise response for application in common high-resolution multi-dimensional biomolecular NMR experiments with water signal suppression on aqueous and salty samples. The method requires the adjustment of the...