Document Detail


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