Protein dynamics detected in a membrane-embedded potassium channel using two-dimensional solid-state NMR spectroscopy期刊界 All Journals 搜尽天下杂志传播学术成果专业期刊搜索期刊信息化学术搜索

Protein dynamics detected in a membrane-embedded potassium channel using two-dimensional solid-state NMR spectroscopy

Authors:	Christian Ader Stefan Becker

Affiliation:	^a Bijvoet Center for Biomolecular Research, Utrecht University, Padualaan 8, 3584 CH Utrecht, The Netherlands ^b Universität Hamburg, Zentrum für Molekulare Neurobiologie, Institut für Neurale Signalverarbeitung, Falkenried 94, 20251 Hamburg, Germany ^c Max-Planck-Institute for Biophysical Chemistry, Department of NMR-based Structural Biology, Am Fassberg 11, 37077 Göttingen, Germany

Abstract:	We report longitudinal ¹⁵N relaxation rates derived from two-dimensional (¹⁵N, ¹³C) chemical shift correlation experiments obtained under magic angle spinning for the potassium channel KcsA-Kv1.3 reconstituted in multilamellar vesicles. Thus, we demonstrate that solid-state NMR can be used to probe residue-specific backbone dynamics in a membrane-embedded protein. Enhanced backbone mobility was detected for two glycine residues within the selectivity filter that are highly conserved in potassium channels and that are of core relevance to the filter structure and ion selectivity.

Keywords:	Dynamics Ion channel MAS Membrane Protein Solid-state NMR
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