Rapid solid-state NMR of deuterated proteins by interleaved cross-polarization from 1H and 2H nuclei

We present a novel sampling strategy, interleaving acquisition of multiple NMR spectra by exploiting initial polarization subsequently from H-1 and H-2 spins, taking advantage of their different T-1 relaxation times. Different H-1- and H-2-polarization based spectra are in this way simultaneously recorded improving either information content or sensitivity by adding spectra. The so-called Relaxation-optimized Acquisition of Proton Interleaved with Deuterium (RAPID) H-1 -> C-13/H-2 -> C-13 CP/MAS multiple-acquisition method is demonstrated by 1D and 2D experiments using a uniformly H-2, N-15, C-13-labeled alpha-spectrin SH3 domain sample with all or 30% back-exchanged labile H-2 to H-1. It is demonstrated how 1D C-13 CP/MAS or 2D C-13-C-13 correlation spectra initialized with polarization from either H-1 or H-2 may be recorded simultaneously with flexibility to be added or used individually for spectral editing. It is also shown how 2D C-13-C-13 correlation spectra may be recorded interleaved with H-2-C-13 correlation spectra to obtain C-13-C-13 correlations along with information about dynamics from H-2 sideband patterns. (C) 2011 Elsevier Inc. All rights reserved.