Covalent modification of an exposed surface turn alters the global conformation of the biotin carrier domain of Escherichia coli acetyl-CoA carboxylase

Journal of Biological Chemistry

Volumn 272, Issue 41, 1997, Pages 26017-26022

  Chapman Smith, Anne ^a   Forbes, Briony E ^a   Wallace, John C ^a   Cronan Jr , John E ^b  

^a UNIVERSITY OF ADELAIDE   (Australia)

^b UNIVERSITY OF ILLINOIS AT URBANA CHAMPAIGN   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BIOTIN; CARRIER PROTEIN;

ARTICLE; CARBOXY TERMINAL SEQUENCE; DISULFIDE BOND; ENZYME ACTIVITY; ESCHERICHIA COLI; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN CONFORMATION; PROTEIN DENATURATION;

ACETYL-COA CARBOXYLASE; AMINO ACID SEQUENCE; BINDING SITES; BIOTINYLATION; CARRIER PROTEINS; CHROMATOGRAPHY, HIGH PRESSURE LIQUID; ESCHERICHIA COLI; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PEPTIDE FRAGMENTS; PROTEIN CONFORMATION; SURFACE PROPERTIES;

ESCHERICHIA COLI;

EID: 0030868266     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.272.41.26017     Document Type: Article

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