ArticleBiomolecular NMR assignments2012
Solid-state NMR [13C,15N] resonance assignments of the nucleotide-binding domain of a bacterial cyclic nucleotide-gated channel.
Article in Biomolecular NMR assignments, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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3 citing papers in PubMed.
- Bidirectional band-selective magnetization transfer along the protein backbone doubles the information content of solid-state NMR correlation experiments.Journal of biomolecular NMR · 2017Article
- Efficient and stable reconstitution of the ABC transporter BmrA for solid-state NMR studies.Frontiers in molecular biosciences · 2014Article
- Rapid prediction of multi-dimensional NMR data sets.Journal of biomolecular NMR · 2012Article
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6 authors.
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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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