Solid-state NMR [(13)C, (15)N] resonance assignments of the nucleotide-binding 
domain of a bacterial cyclic nucleotide-gated channel

Cukkemane, A.; Nand, D.; Gradmann, S.; Weingarth, M.; Kaupp, U. B.; Baldus, M.

doi:10.1007/s12104-012-9363-4

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Solid-state NMR [(13)C, (15)N] resonance assignments of the nucleotide-binding domain of a bacterial cyclic nucleotide-gated channel

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Cukkemane, A.
Department of Molecular Sensory Systems, Center of Advanced European Studies and Research (caesar), Max Planck Society;

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Kaupp, U. B.
Department of Molecular Sensory Systems, Center of Advanced European Studies and Research (caesar), Max Planck Society;

Externe Ressourcen

http://www.ncbi.nlm.nih.gov/pubmed/22302441
(beliebiger Volltext)

http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3438399/pdf/12104_2012_Article_9363.pdf
(beliebiger Volltext)

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Zitation

Cukkemane, A., Nand, D., Gradmann, S., Weingarth, M., Kaupp, U. B., & Baldus, M. (2012). Solid-state NMR [(13)C, (15)N] resonance assignments of the nucleotide-binding domain of a bacterial cyclic nucleotide-gated channel. Biomolecular NMR assignments, 6, 225-229. doi:10.1007/s12104-012-9363-4.

Zitierlink: https://hdl.handle.net/11858/00-001M-0000-0028-61E2-A

Zusammenfassung

Channels regulated by cyclic nucleotides are key signalling proteins in several biological pathways. The regulatory aspect is conferred by a C-terminal cyclic nucleotide-binding domain (CNBD). We report resonance assignments of the CNBD of a bacterial mlCNG channel obtained using 2D and 3D solid-state NMR under Magic-angle Spinning conditions. A secondary chemical shift analysis of the 141 residue protein suggests a three-dimensional fold seen in earlier X-ray and solution-state NMR work and points to spectroscopic polymorphism for a selected set of resonances.