Fast Resonance Assignment and Fold Determination of Human Superoxide Dismutase by High-Resolution Proton-Detected Solid-State MAS NMR Spectroscopy

Knight, Michael J.Webber, Amy L.Pell, Andrew J.Guerry, PaulBarbet-Massin, EmelineBertini, IvanoFelli, Isabella C.Gonnelli, LeonardoPierattelli, RobertaEmsley, LyndonLesage, AnneHerrmann, TorstenPintacuda, Guido2015-01-082015-01-082015-01-08201110.1002/anie.201106340https://infoscience.epfl.ch/handle/20.500.14299/110010WOS:000298084900024Re-protonation is key: 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 (ZnII-SOD) fully [ 2H,13C,15N]-labeled and 100% re-protonated at the exchangeable sites. Copyright © 2011 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.1H detectionNMR spectroscopyprotein structurestructural constraintsFast Resonance Assignment and Fold Determination of Human Superoxide Dismutase by High-Resolution Proton-Detected Solid-State MAS NMR Spectroscopytext::journal::journal article::research article