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Chemphyschem. 2014 Jun 23;15(9):1872-9. doi: 10.1002/cphc.201301232. Epub 2014 Apr 30.

Spatially selective heteronuclear multiple-quantum coherence spectroscopy for biomolecular NMR studies.

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Department of Chemistry, The State University of New York at Buffalo, Buffalo NY 14260 (USA); Present address: Department of Biophysics and Chemistry, University of Michigan, Ann Arbor, MI 48108 (USA).


Spatially selective heteronuclear multiple-quantum coherence (SS HMQC) NMR spectroscopy is developed for solution studies of proteins. Due to "time-staggered" acquisitioning of free induction decays (FIDs) in different slices, SS HMQC allows one to use long delays for longitudinal nuclear spin relaxation at high repetition rates. To also achieve high intrinsic sensitivity, SS HMQC is implemented by combining a single spatially selective (1)H excitation pulse with nonselective (1) H 180° pulses. High-quality spectra were obtained within 66 s for a 7.6 kDa uniformly (13) C,(15) N-labeled protein, and within 45 and 90 s for, respectively, two proteins with molecular weights of 7.5 and 43 kDa, which were uniformly (2)H,(13) C,(15) N-labeled, except for having protonated methyl groups of isoleucine, leucine and valine residues.


HMQC; flip-back pulses; rapid data acquisition; spatially selective NMR; time-staggered data acquisition

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