Long-range correlations between aliphatic 13C nuclei in protein MAS NMR spectroscopy

Abstract

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. © 2009 Wiley-VCH Verlag GmbH & Co. KGaA.