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Updated: Jun 27, 2026

Neutron Crystallography Data Collection and Processing for Modelling Hydrogen Atoms in Protein Structures
Published on: December 1, 2020
High-resolution double-quantum deuterium magic angle spinning solid-state NMR spectroscopy of perdeuterated proteins
Vipin Agarwal1, Katja Faelber, Peter Schmieder
1Leibniz-Institut fur Molekulare Pharmakologie (FMP), Robert-Rossle-Strasse 10, 13125 Berlin, Germany.
Abstract:
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.
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