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Updated: Apr 30, 2026

Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy
Published on: September 17, 2017
Spatially selective heteronuclear multiple-quantum coherence spectroscopy for biomolecular NMR studies
Bharathwaj Sathyamoorthy1, David M Parish, Gaetano T Montelione
1Department 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).
Abstract:
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.
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