Narrow carbonyl resonances in proton-diluted proteins facilitate NMR assignments in the solid-state.
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.
Leibniz-Institut für Molekulare Pharmakologie, Robert-Rössle Str. 10, 13125, Berlin, Germany.
Rasmus
R
Linser
Uwe
U
Fink
Bernd
B
Reif
D000818:Animals; D002247:Carbon Isotopes / Q000737:chemistry; D002645:Chickens; D003903:Deuterium / Q000737:chemistry; D009587:Nitrogen Isotopes / Q000737:chemistry; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods*; D010100:Oxygen / Q000737:chemistry; D011506:Proteins / Q000737:chemistry*; D013049:Spectrin / Q000737:chemistry; D018909:src Homology Domains
D002247:Carbon Isotopes; D009587:Nitrogen Isotopes; D011506:Proteins; D013049:Spectrin; D003903:Deuterium; D010100:Oxygen