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Updated: Jun 15, 2026

Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy
Published on: September 17, 2017
Narrow carbonyl resonances in proton-diluted proteins facilitate NMR assignments in the solid-state
Rasmus Linser1, Uwe Fink, Bernd Reif
1Leibniz-Institut für Molekulare Pharmakologie, Robert-Rössle Str. 10, 13125, Berlin, Germany.
Abstract:
HNCO/HNCACO type correlation experiments are an alternative for assignment of backbone resonances in extensively deuterated proteins in the solid-state, given the fact that line widths on the order of 14-17 Hz are achieved in the carbonyl dimension without the need of high power decoupling. The achieved resolution demonstrates that MAS solid-state NMR on extensively deuterated proteins is able to compete with solution-state NMR spectroscopy if proteins are investigated with correlation times tau(c) that exceed 25 ns.
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