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Wiley, Angewandte Chemie International Edition, 7(46), p. 1079-1082, 2007

DOI: 10.1002/anie.200603093

Wiley, Angewandte Chemie, 7(119), p. 1097-1100, 2007

DOI: 10.1002/ange.200603093

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Solid-State NMR Spectroscopy of a Paramagnetic Protein: Assignment and Study of Human Dimeric Oxidized CuII–ZnII Superoxide Dismutase (SOD)

Journal article published in 2007 by Guido Pintacuda, Nicolas Giraud ORCID, Roberta Pierattelli ORCID, Anja Böckmann, Ivano Bertini, Lyndon Emsley
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This paper is available in a repository.

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Abstract

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 (13C-15N NMR correlation spectrum shown in background). (Figure Presented).