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Default Cardiolipin Interaction with Subunit c of ATP synthase: Solid-state NMR Characterization.

Cardiolipin Interaction with Subunit c of ATP synthase: Solid-state NMR Characterization.

Related Articles Cardiolipin Interaction with Subunit c of ATP synthase: Solid-state NMR Characterization.

Biochim Biophys Acta. 2014 Aug 25;

Authors: Laage S, Tao Y, McDermott AE

Abstract
The interaction of lipids with subunit c from F1Fo ATP synthase are studied by biophysical methods. Subunit c from both Escherichia coli and Streptococcus pneumoniae interact and copurify with cardiolipin. Solid state NMR data on oligomeric rings of Fo show that the cardiolipin interacts with the c subunits in membrane bilayers. These studies offer strong support for the hypothesis that Fo has specific interactions with cardiolipin. This article is part of a Special Issue entitled: NMR Spectroscopy for Atomistic Views of Biomembranes and Cell Surfaces.


PMID: 25168468 [PubMed - as supplied by publisher]



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