Spectral editing of alanine, serine, and threonine in uniformly labeled proteins based on frequency-selective homonuclear recoupling in solid-state NMR.
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DOI: 10.1007/s10858-021-00367-9
Abstract: Spectral editing is crucial to simplify the crowded solid-state NMR spectra of proteins. New techniques are introduced to edit 13C-13C correlations of uniformly labeled proteins under moderate magic-angle spinning (MAS), based on our recent frequency-selective… read more here.
Keywords: solid state; labeled proteins; state nmr; spectral editing ... See more keywords