Narrow carbonyl resonances in proton-diluted proteins facilitate NMR assignments in t
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 14â??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 Ï? c that exceed 25 ns.
Content Type Journal Article
DOI 10.1007/s10858-010-9404-1
Authors
Rasmus Linser, Leibniz-Institut für Molekulare Pharmakologie (FMP) Robert-Rössle Str. 10 13125 Berlin Germany
Uwe Fink, Leibniz-Institut für Molekulare Pharmakologie (FMP) Robert-Rössle Str. 10 13125 Berlin Germany
Bernd Reif, Leibniz-Institut für Molekulare Pharmakologie (FMP) Robert-Rössle Str. 10 13125 Berlin Germany
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Narrow carbonyl resonances in proton-diluted proteins facilitate NMR assignments in t
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