Thursday, January 08, 2009

J. Am. Chem. Soc., 2009, 131 (1), pp 2–3

High-Resolution Double-Quantum Deuterium Magic Angle Spinning Solid-State NMR Spectroscopy of Perdeuterated Proteins

Vipin Agarwal†, Katja Faelber†, Peter Schmieder† and Bernd Reif*‡


We show in this manuscript that 2H,13C correlation spectra in uniformly 2H,13C isotopically enriched peptides and proteins can be recorded in MAS solid-state NMR with site specific resolution. A resolved deuterium dimension is obtained by evolving 2H double-quantum coherences. Experimental 2H line widths are obtained that are as small as 16 Hz (0.17 ppm at 600 MHz) in the double-quantum dimension. The unprecedented resolution in the deuterium dimension obtained for proteins opens new perspectives for correlation experiments and, in particular, for the characterization of dynamics of proteins in the solid-state.

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