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Springer (part of Springer Nature), Journal of Biomolecular NMR, 1(47), p. 1-6

DOI: 10.1007/s10858-010-9404-1

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Narrow carbonyl resonances in proton-diluted proteins facilitate NMR assignments in the solid-state.

Journal article published in 2010 by Rasmus Linser, Uwe Fink, Bernd Reif ORCID
This paper is available in a repository.
This paper is available in a repository.

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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.