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Solid‐State NMR Spectroscopy of a Paramagnetic Protein: Assignment and Study of Human Dimeric Oxidized Cu II –Zn II Superoxide Dismutase (SOD)
Author(s) -
Pintacuda Guido,
Giraud Nicolas,
Pierattelli Roberta,
Böckmann Anja,
Bertini Ivano,
Emsley Lyndon
Publication year - 2007
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.200603093
Subject(s) - chemistry , paramagnetism , superoxide dismutase , magic angle spinning , microcrystalline , dimer , crystallography , spectroscopy , nuclear magnetic resonance spectroscopy , nuclear magnetic resonance , physics , stereochemistry , enzyme , biochemistry , condensed matter physics , organic chemistry , quantum mechanics
A solid story : The paramagnetic form of the protein superoxide dismutase (SOD; see portion of structure in upper right corner of picture with detectability sphere in blue) is shown to be accessible to high‐resolution solid‐state magic angle spinning NMR studies when in microcrystalline form. A nearly complete assignment of the signals of this 32‐kDa dimer has been achieved ( 13 C– 15 N NMR correlation spectrum shown in background).