High-resolution double-quantum deuterium magic angle spinning solid-state NMR spectroscopy of perdeuterated proteins.
We show in this manuscript that (2)H,(13)C correlation spectra in uniformly (2)H,(13)C 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 (2)H double-quantum coherences. Experimental (2)H 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.
Agarwal
Vipin
V
Leibniz-Institut fur Molekulare Pharmakologie (FMP), Robert-Rossle-Strasse 10, 13125 Berlin, Germany.
Faelber
Katja
K
Schmieder
Peter
P
Reif
Bernd
B
D000818:Animals; D002247:Carbon Isotopes; D002645:Chickens; D003903:Deuterium; D004151:Dipeptides / Q000737:chemistry; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods*; D011789:Quantum Theory; D013049:Spectrin / Q000737:chemistry*; D018909:src Homology Domains
D002247:Carbon Isotopes; D004151:Dipeptides; D013049:Spectrin; D003903:Deuterium