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

Standard

Protein dynamics detected in a membrane-embedded potassium channel using two-dimensional solid-state NMR spectroscopy. / Ader, Christian; Pongs, Olaf; Becker, Stefan; Baldus, Marc.

in: BBA-BIOMEMBRANES, Jahrgang 1798, Nr. 2, 2, 2010, S. 286-290.

Publikationen: SCORING: Beitrag in Fachzeitschrift/Zeitung › SCORING: Zeitschriftenaufsatz › Forschung › Begutachtung

Harvard

Ader, C, Pongs, O, Becker, S & Baldus, M 2010, 'Protein dynamics detected in a membrane-embedded potassium channel using two-dimensional solid-state NMR spectroscopy.', BBA-BIOMEMBRANES, Jg. 1798, Nr. 2, 2, S. 286-290. <http://www.ncbi.nlm.nih.gov/pubmed/19595989?dopt=Citation>

APA

Ader, C., Pongs, O., Becker, S., & Baldus, M. (2010). Protein dynamics detected in a membrane-embedded potassium channel using two-dimensional solid-state NMR spectroscopy. BBA-BIOMEMBRANES, 1798(2), 286-290. [2]. http://www.ncbi.nlm.nih.gov/pubmed/19595989?dopt=Citation

Vancouver

Ader C, Pongs O, Becker S, Baldus M. Protein dynamics detected in a membrane-embedded potassium channel using two-dimensional solid-state NMR spectroscopy. BBA-BIOMEMBRANES. 2010;1798(2):286-290. 2.

Bibtex

@article{790cca69917c47a583c40c6372370429,
title = "Protein dynamics detected in a membrane-embedded potassium channel using two-dimensional solid-state NMR spectroscopy.",
abstract = "We report longitudinal (15)N relaxation rates derived from two-dimensional ((15)N, (13)C) 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.",
author = "Christian Ader and Olaf Pongs and Stefan Becker and Marc Baldus",
year = "2010",
language = "Deutsch",
volume = "1798",
pages = "286--290",
journal = "BBA-BIOMEMBRANES",
issn = "0005-2736",
publisher = "Elsevier",
number = "2",

}

RIS

TY - JOUR

T1 - Protein dynamics detected in a membrane-embedded potassium channel using two-dimensional solid-state NMR spectroscopy.

AU - Ader, Christian

AU - Pongs, Olaf

AU - Becker, Stefan

AU - Baldus, Marc

PY - 2010

Y1 - 2010

N2 - We report longitudinal (15)N relaxation rates derived from two-dimensional ((15)N, (13)C) 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.

AB - We report longitudinal (15)N relaxation rates derived from two-dimensional ((15)N, (13)C) 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.

M3 - SCORING: Zeitschriftenaufsatz

VL - 1798

SP - 286

EP - 290

JO - BBA-BIOMEMBRANES

JF - BBA-BIOMEMBRANES

SN - 0005-2736

IS - 2

M1 - 2

ER -