| Cardiolipin Interaction with Subunit c of ATP synthase: Solid-state NMR Characterization. | |
MedLine Citation:
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PMID: 25168468 Owner: NLM Status: Publisher |
Abstract/OtherAbstract:
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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. |
Authors:
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Ségolène Laage; Yisong Tao; Ann E McDermott |
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Publication Detail:
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Type: JOURNAL ARTICLE Date: 2014-8-25 |
Journal Detail:
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Title: Biochimica et biophysica acta Volume: - ISSN: 0006-3002 ISO Abbreviation: Biochim. Biophys. Acta Publication Date: 2014 Aug |
Date Detail:
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Created Date: 2014-8-29 Completed Date: - Revised Date: - |
Medline Journal Info:
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Nlm Unique ID: 0217513 Medline TA: Biochim Biophys Acta Country: - |
Other Details:
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Languages: ENG Pagination: - Citation Subset: - |
Copyright Information:
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Copyright © 2014. Published by Elsevier B.V. |
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