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

Linser, R.; Fink, U.; Reif, B.

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.

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Linser, R.
Research Group of Solid-State NMR-2, MPI for Biophysical Chemistry, Max Planck Society;

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Citation

Linser, R., Fink, U., & Reif, B. (2010). Narrow carbonyl resonances in proton-diluted proteins facilitate NMR assignments in the solid-state. Journal of Biomolecular NMR, 47(1), 1-6. doi:10.1007/s10858-010-9404-1.

Cite as: https://hdl.handle.net/11858/00-001M-0000-0018-EB11-A

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 τ c that exceed 25 ns.