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Solid-state NMR [13C,15N] resonance assignments of the nucleotide-Binding Domain of a bacterial Cyclic Nucleotide-Gated Channel

By A.A. Cukkemane, D. Nand, S.H.E. Gradmann, M.H. Weingarth, U.B. Kaupp and M. Baldus


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 Magicangle Spinning conditions. A secondary chemical shift analysis of the 141 residue protein suggests a threedimensional fold seen in earlier X-ray and solution-state NMR work and points to spectroscopic polymorphism for a selected set of resonances

Year: 2012
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