Abstract
TROSY-type optimization of liquid-state NMR experiments is based on the preservation of unique coherence transfer pathways with distinct transverse relaxation properties. The broadband decoupling of the 1H spins interchanges the TROSY and anti-TROSY magnetization transfer pathways and thus is not used in TROSY-type triple resonance experiments or is replaced with narrowband selective decoupling. To achieve the full advantage of TROSY, the uniform deuteration of proteins is usually required. Here we propose a new and general method for 1H broadband decoupling in TROSY NMR, which does not compromise the relaxation optimization in the 15N–1H moieties, but uniformly and efficiently refocuses the 1 J CH scalar coupling evolution in the 13C–1H moieties. Combined with the conventional 2H decoupling, this method enables obtaining high sensitivity TROSY-type triple resonance spectra with partially deuterated or fully protonated 13C,15N labeled proteins.
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Eletsky, A., Kienhöfer, A. & Pervushin, K. TROSY NMR with partially deuterated proteins. J Biomol NMR 20, 177–180 (2001). https://doi.org/10.1023/A:1011265430149
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DOI: https://doi.org/10.1023/A:1011265430149