A solid story: The paramagnetic form of the protein superoxide dismutase 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).
Solid-state NMR spectroscopy of a paramagnetic protein: assignment and study of human dimeric oxidized Cu(II), Zn(II) superoxide dismutase (SOD) / G.Pintacuda; N.Giraud; R.Pierattelli; A.Boeckmann; I.Bertini; L.Emsley. - In: ANGEWANDTE CHEMIE. INTERNATIONAL EDITION. - ISSN 1433-7851. - STAMPA. - 46:(2007), pp. 1079-1082. [10.1002/anie.200603093]
Solid-state NMR spectroscopy of a paramagnetic protein: assignment and study of human dimeric oxidized Cu(II), Zn(II) superoxide dismutase (SOD).
PIERATTELLI, ROBERTA;BERTINI, IVANO;
2007
Abstract
A solid story: The paramagnetic form of the protein superoxide dismutase 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).File | Dimensione | Formato | |
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Solid-state NMR spectroscopy of a paramagnetic protein assignment and study of human dimeric oxidized CuIIZnII superoxide dismutase SOD.pdf
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