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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

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.

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Item Permalink: https://hdl.handle.net/11858/00-001M-0000-0028-61E2-A Version Permalink: https://hdl.handle.net/11858/00-001M-0000-0028-61E3-8
Genre: Journal Article

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Cukkemane_Solid-state.pdf (Any fulltext), 476KB
 
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http://www.ncbi.nlm.nih.gov/pubmed/22302441 (Any fulltext)
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http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3438399/pdf/12104_2012_Article_9363.pdf (Any fulltext)
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 Creators:
Cukkemane, A.1, Author           
Nand, D., Author
Gradmann, S., Author
Weingarth, M., Author
Kaupp, U. B.1, Author           
Baldus, M., Author
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1Department of Molecular Sensory Systems, Center of Advanced European Studies and Research (caesar), Max Planck Society, ou_2173679              

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 Abstract: 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.

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 Dates: 2012
 Publication Status: Issued
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 Identifiers: Other: 22302441
DOI: 10.1007/s12104-012-9363-4
ISSN: 1874-270X (Electronic)
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Title: Biomolecular NMR assignments
  Alternative Title : Biomol. NMR Assign.
Source Genre: Journal
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Pages: - Volume / Issue: 6 Sequence Number: - Start / End Page: 225 - 229 Identifier: -