Solid-state NMR 13C,15N resonance assignments of the nucleotide-binding domain of a bacterial cyclic nucleotide-gated channelReport as inadecuate




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Biomolecular NMR Assignments

, Volume 6, Issue 2, pp 225–229

First Online: 03 February 2012Received: 27 October 2011Accepted: 17 January 2012

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.

KeywordsCyclic nucleotide-binding domain Cyclic AMP Solid-state NMR Magic-angle Spinning Electronic supplementary materialThe online version of this article doi:10.1007-s12104-012-9363-4 contains supplementary material, which is available to authorized users.

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Author: Abhishek Cukkemane - Deepak Nand - Sabine Gradmann - Markus Weingarth - U. Benjamin Kaupp - Marc Baldus

Source: https://link.springer.com/







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