The ε subunit of the F1F0 complex of Escherichia coli. Cross-linking studies show the same structure in situ as when isolated

Journal of Biological Chemistry

Volumn 274, Issue 40, 1999, Pages 28351-28355

  Schulenberg, Birte ^a   Capaldi, Roderick A ^a  

^a UNIVERSITY OF OREGON   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATE; ADENYLYLIMIDODIPHOSPHATE; COPPER CHLORIDE; CYSTEINE; DICYCLOHEXYLCARBODIIMIDE; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATE SYNTHASE; ADENINE NUCLEOTIDE; CROSS LINKING REAGENT; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATASE; TRYPSIN;

ALPHA HELIX; ARTICLE; CARBOXY TERMINAL SEQUENCE; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; DISULFIDE BOND; ENZYME STRUCTURE; ENZYME SUBUNIT; ESCHERICHIA COLI; HYDROLYSIS; NONHUMAN; PRIORITY JOURNAL; PROTEIN CROSS LINKING; PROTEIN DOMAIN; SITE DIRECTED MUTAGENESIS; CHEMISTRY; ENZYMOLOGY; GENETICS; METABOLISM; PROTEIN CONFORMATION;

ADENINE NUCLEOTIDES; CROSS-LINKING REAGENTS; ESCHERICHIA COLI; HYDROLYSIS; MUTAGENESIS, SITE-DIRECTED; PROTEIN CONFORMATION; PROTON-TRANSLOCATING ATPASES; TRYPSIN;

EID: 0033201448     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.274.40.28351     Document Type: Article

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