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Article

Conformational dynamics of the Na+/K+-ATPase probed by voltage clamp fluorometry.

Proceedings of the National Academy of Sciences of the United States of America - 4 Feb 2003

Geibel Sven, Kaplan Jack H, Bamberg Ernst, Friedrich Thomas

Abstract excerpt

The method of voltage clamp fluorometry combined with site-directed fluorescence labeling was used to detect local protein motions of the fully active Na(+)K(+)-ATPase in real time under physiological conditions. Because helix M5 extends from the cytoplasmic site of ATP hydrolysis into the cation binding region, we chose the extracellular M5-M6 loop of the sheep alpha(1)-subunit for the insertion of cysteine...

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Identifiers

PMID: 12552111
DOI: 10.1073/pnas.0337336100
PMCID: PMC298709

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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