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Fast Resonance Assignment and Fold Determination of Human Superoxide Dismutase by High‐Resolution Proton‐Detected Solid‐State MAS NMR Spectroscopy
Author(s) -
Knight Michael J.,
Webber Amy L.,
Pell Andrew J.,
Guerry Paul,
BarbetMassin Emeline,
Bertini Ivano,
Felli Isabella C.,
Gonnelli Leonardo,
Pierattelli Roberta,
Emsley Lyndon,
Lesage Anne,
Herrmann Torsten,
Pintacuda Guido
Publication year - 2011
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201106340
Subject(s) - microcrystalline , protonation , magic angle spinning , superoxide dismutase , chemistry , high resolution , spectroscopy , nuclear magnetic resonance spectroscopy , low resolution , analytical chemistry (journal) , nuclear magnetic resonance , crystallography , stereochemistry , physics , biochemistry , chromatography , enzyme , organic chemistry , ion , remote sensing , quantum mechanics , geology
Re‐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 (Zn II ‐SOD) fully [ 2 H, 13 C, 15 N]‐labeled and 100 % re‐protonated at the exchangeable sites.