Phospholipids occupy the internal lumen of the c ring of the ATP synthase of Escherichia coli

Biochemistry

Volumn 45, Issue 6, 2006, Pages 1841-1851

  Oberfeld, Benjamin ^a   Brunner, Josef ^a   Dimroth, Peter ^a  

^a ETH ZURICH   (Switzerland)

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINETRIPHOSPHATE; ALKYLATION; BIOLOGICAL MEMBRANES; PHOSPHOLIPIDS; SPECTROSCOPIC ANALYSIS;

ATP SYNTHASE; MEMBRANE-EMBEDDED C RING; PHOTO-CROSS-LINKING APPROACH; SINGLE CYSTEINE MUTANTS;

ESCHERICHIA COLI;

DIACYLGLYCEROL; PHOSPHATIDYLETHANOLAMINE; PHOSPHOLIPASE C; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATE SYNTHASE;

ALKYLATION; ARTICLE; CONFORMATIONAL TRANSITION; CROSS LINKING; DRUG ISOLATION; ENZYME SUBUNIT; ESCHERICHIA COLI; LIPID BILAYER; MASS SPECTROMETRY; MEMBRANE POTENTIAL; NONHUMAN; PHOSPHOLIPID MEMBRANE; PHOTOACTIVATION; PRIORITY JOURNAL; RECEPTOR OCCUPANCY;

ALKYLATION; ATP SYNTHETASE COMPLEXES; BASE SEQUENCE; BINDING SITES; CELL MEMBRANE; CROSS-LINKING REAGENTS; CYSTEINE; DIGLYCERIDES; ESCHERICHIA COLI; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; PHOSPHATIDYLETHANOLAMINES; PHOSPHOLIPASE C; PHOSPHOLIPIDS; PHOTOCHEMISTRY; PROTEIN CONFORMATION; PROTEIN SUBUNITS; SPECTROMETRY, MASS, MATRIX-ASSISTED LASER DESORPTION-IONIZATION;

ESCHERICHIA COLI;

EID: 32344451446     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi052304+     Document Type: Article

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