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Issue 22, 2004
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Protein solid-state NMR resonance assignments from (13C,13C) correlation spectroscopy

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Abstract

It is demonstrated that sequential resonance assignments can be obtained from (13C,13C) correlation spectroscopy on a uniformly labeled protein under magic angle spinning. The experiment relies on weak (C′,Cα) coupling conditions using a defined range of MAS rates and can be employed at arbitrary magnetic field strength.

Graphical abstract: Protein solid-state NMR resonance assignments from (13C,13C) correlation spectroscopy

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Publication details

The article was received on 30 Jul 2004, accepted on 28 Sep 2004 and first published on 08 Oct 2004


Article type: Communication
DOI: 10.1039/B411689E
Citation: Phys. Chem. Chem. Phys., 2004,6, 5090-5093
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    Protein solid-state NMR resonance assignments from (13C,13C) correlation spectroscopy

    K. Seidel, A. Lange, S. Becker, C. E. Hughes, H. Heise and M. Baldus, Phys. Chem. Chem. Phys., 2004, 6, 5090
    DOI: 10.1039/B411689E

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