TROSY NMR with partially deuterated proteins

摘要: TROSY-type optimization of liquid-state NMR experiments is based on the preservation unique coherence transfer pathways with distinct transverse relaxation properties. The broadband decoupling 1H spins interchanges TROSY and anti-TROSY magnetization thus not used in triple resonance or replaced narrowband selective decoupling. To achieve full advantage TROSY, uniform deuteration proteins usually required. Here we propose a new general method for NMR, which does compromise 15N-1H moieties, but uniformly efficiently refocuses 1JCH scalar coupling evolution 13C-1H moieties. Combined conventional 2H decoupling, this enables obtaining high sensitivity spectra partially deuterated fully protonated 13C,15N labeled proteins.