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

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  • Financial support by the Access to Research Infrastructures activity in the 6th Framework Programme of the EC (contract no. RII3-026145, EU-NMR) and from the French National Research Agency is gratefully acknowledged (ANR JC 2005). Financial support from the Ministero dell'Istruzione, dell'Università e della Ricerca (COFIN 2005, prot. no. 2005039878) and Ente Cassa di Risparmio di Firenze is acknowledged.

Abstract

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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).

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