Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
1944810 | Biochimica et Biophysica Acta (BBA) - Biomembranes | 2010 | 5 Pages |
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.
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Authors
Christian Ader, Olaf Pongs, Stefan Becker, Marc Baldus,