A combination of a high magnetic field (1 GHz) and ultra-fast magic-angle spinning (60 kHz) allows easy detection of NMR spectra revealing details of secondary and tertiary structures of medium-sized proteins. The technique was applied to the 153-residue microcrystalline Zn(II)-loaded superoxide dismutase fully [2H,13C,15N]-labeled and 100 % re-protonated at the exchangeable sites.
Fast resonance assignment and fold determination of human superoxide dismutase by high-resolution proton-detected solid state MAS NMR spectroscopy / M.J.Knight; A.L.Webber; A.J.Pell; P.Guerry; E.Barbet-Massin; I.Bertini; I.C.Felli; L.Gonnelli; R.Pierattelli; L.Emsley; A.Lesage; T.Hermann; G.Pintacuda. - In: ANGEWANDTE CHEMIE. INTERNATIONAL EDITION. - ISSN 1433-7851. - STAMPA. - 50:(2011), pp. 11697-11701. [10.1002/anie.201106340]
Fast resonance assignment and fold determination of human superoxide dismutase by high-resolution proton-detected solid state MAS NMR spectroscopy
BERTINI, IVANO;FELLI, ISABELLA CATERINA;GONNELLI, LEONARDO;PIERATTELLI, ROBERTA;
2011
Abstract
A combination of a high magnetic field (1 GHz) and ultra-fast magic-angle spinning (60 kHz) allows easy detection of NMR spectra revealing details of secondary and tertiary structures of medium-sized proteins. The technique was applied to the 153-residue microcrystalline Zn(II)-loaded superoxide dismutase fully [2H,13C,15N]-labeled and 100 % re-protonated at the exchangeable sites.
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