Publication date: Available online 7 May 2015 Source:Journal of Magnetic Resonance
Author(s): Joshua I. Friedman , Ding Xia , Ravinder R. Regatte , Alexej Jerschow
Chemical Exchange Saturation Transfer (CEST) magnetic resonance experiments have become valuable tools in magnetic resonance for the detection of low concentration solutes with far greater sensitivity than direct detection methods. Accurate measures of rates of chemical exchange provided by CEST are of particular interest to biomedical imaging communities where variations in chemical exchange can be related to subtle variations in biomarker concentration, temperature and pH within tissue using MRI. Despite their name, however, traditional CEST methods are not truly selective for chemical exchange and instead detect all forms of magnetization transfer including through-space NOE. This ambiguity crowds CEST spectra and greatly complicates subsequent data analysis. We have developed a Transfer Rate Edited CEST experiment (TRE-CEST) that uses two different types of solute labeling in order to selectively amplify signals of rapidly exchanging proton species while simultaneously suppressing ‘slower’ NOE-dominated magnetization transfer processes. This approach is demonstrated in the context of both NMR and MRI, where it is used to detect the labile amide protons of proteins undergoing chemical exchange (at rates ? 30 s-1) while simultaneously eliminating signals originating from slower (~ 5 s-1) NOE-mediated magnetization transfer processes. TRE-CEST greatly expands the utility of CEST experiments in complex systems, and in-vivo, in particular, where it is expected to improve the quantification of chemical exchange and magnetization transfer rates while enabling new forms of imaging contrast. Graphical abstract
[NMR paper] Probing the rate limiting step for intramolecular transfer of a transcription factor between specific sites on the same DNA molecule by 15Nz-exchange NMR spectroscopy.
Probing the rate limiting step for intramolecular transfer of a transcription factor between specific sites on the same DNA molecule by 15Nz-exchange NMR spectroscopy.
Related Articles Probing the rate limiting step for intramolecular transfer of a transcription factor between specific sites on the same DNA molecule by 15Nz-exchange NMR spectroscopy.
J Am Chem Soc. 2014 Sep 25;
Authors: Ryu KS, Tugarinov V, Clore GM
Abstract
The kinetics of translocation of the homeodomain transcription factor HoxD9 between specific sites of...
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09-26-2014 01:03 PM
HNCA+, HNCO+, and HNCACB+ experiments: improved performance by simultaneous detection of orthogonal coherence transfer pathways
HNCA+, HNCO+, and HNCACB+ experiments: improved performance by simultaneous detection of orthogonal coherence transfer pathways
Abstract
Three experiments, BESTâ??TROSY HNCA+, HNCO+ and HNCACB+ are presented for sequential backbone resonance assignment of 13C, 15N labelled proteins. The novelty of these experiments with respect to conventional pulse sequences is the detection of additional orthogonal coherence transfer pathways that results in enhanced sensitivity for sequential correlations without significantly compromising the intensity of...
Characterizing Slow Chemical Exchange in Nucleic Acids by Carbon CEST and Low Spin-Lock Field R1? NMR Spectroscopy
Characterizing Slow Chemical Exchange in Nucleic Acids by Carbon CEST and Low Spin-Lock Field R1? NMR Spectroscopy
Bo Zhao, Alexandar L. Hansen and Qi Zhang
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja409835y/aop/images/medium/ja-2013-09835y_0005.gif
Journal of the American Chemical Society
DOI: 10.1021/ja409835y
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/iu74AOgzY6s
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12-19-2013 05:34 AM
[NMR paper] Efficient CO-CA transfer in highly deuterated proteins by band-selective homonuclear cross-polarization
Efficient CO-CA transfer in highly deuterated proteins by band-selective homonuclear cross-polarization
Available online 14 March 2013
Publication year: 2013
Source:Journal of Magnetic Resonance</br>
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Robust and efficient band-selective magnetization transfer between CO and CA spins can be achieved in highly deuterated solid proteins by dipolar-based homonuclear cross polarization. The approach is designed for moderate magic-angle spinning rates and high external magnetic fields where the isotropic chemical shift difference of CO and CA considerably exceeds the...
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03-16-2013 02:22 AM
[NMR paper] Probing Slow Chemical Exchange at Carbonyl Sites in Proteins by Chemical Exchange Saturation Transfer NMR Spectroscopy.
Probing Slow Chemical Exchange at Carbonyl Sites in Proteins by Chemical Exchange Saturation Transfer NMR Spectroscopy.
Probing Slow Chemical Exchange at Carbonyl Sites in Proteins by Chemical Exchange Saturation Transfer NMR Spectroscopy.
Angew Chem Int Ed Engl. 2013 Feb 28;
Authors: Vallurupalli P, Kay LE
Abstract
Seeing the invisible: A 13 CO NMR chemical exchange saturation transfer (CEST) experiment for the study of "invisible" excited protein states with lifetimes on the order of 5-50 ms has been developed. The 13 CO chemical...
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03-02-2013 11:45 AM
[U. of Ottawa NMR Facility Blog] Saturation Transfer and Exchange
Saturation Transfer and Exchange
Exchange processes that occur on the NMR time scale affect the NMR line shapes and can be studied by line shape analysis. If the exchange process is slow on the NMR time scale, one can employ EXSY or inversion transfer methods to study the exchange. An alternative to these is the saturation transfer technique. In this method, one of the slowly exchanging resonances (A) is saturated with low power CW irradiation and the effect on the intensity of the resonance of the exchange partner (B) is monitored. If there is exchange between A and B during the period of...
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08-03-2011 01:00 AM
TROSY-selected ZZ-exchange experiment for characterizing slow chemical exchange in large proteins
TROSY-selected ZZ-exchange experiment for characterizing slow chemical exchange in large proteins
Abstract A TROSY-selected ZZ-exchange experiment is described for measuring slow chemical exchange rates by monitoring the TROSY component of 15N longitudinal magnetization. Application of the proposed pulse sequence to the cadherin 8 N-terminal extracelluar domain demonstrates that enhanced sensitivity is obtained, compared to a previously described TROSY-detected ZZ-exchange sequence (Sahu et al. J Am Chem Soc 129: 13232â??13237, 2007), by preserving the TROSY effect during the mixing...