Angewandte Chemie International Edition · 2009 · 39 citations · 20 references
Natural SciencesBiochemistryChemistryMagnetic Resonance BiophysicsNuclear ChemistrySpectroscopyMagnetic Resonance Pulse SequencesMagnetic Resonance Signal FormationMagnetic Resonance SpectroscopyProtein StructureSpectroscopy Of BiomoleculesBandwidthCarbon-13 Nuclear Magnetic ResonanceDipolar InteractionsMagnetic Resonance Spectroscopy Of Biomolecules
Highly efficient polarization transfer can be achieved in the magic-angle spinning NMR analysis of proteins by the combination of 13C labeling at alternating positions and band-selective radio-frequency-driven recoupling (BASE RFDR), a pulse scheme aimed at exploiting the bandwidth selectivity and favorable effects of weak 13C radio-frequency irradiation to reintroduce the homonuclear dipolar interactions between distant nuclei.
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Structure of a protein determined by solid-state magic-angle-spinning NMR spectroscopy
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