Conformational changes of the yeast mitochondrial adenosine diphosphate/ adenosine triphosphate carrier studied through its intrinsic fluorescence. 1. Tryptophanyl residues of the carrier can be mutated without impairing protein activity

Biochemistry

Volumn 35, Issue 50, 1996, Pages 16116-16124

  Saux, Agnès Le ^a   Roux, Pierre ^b   Trézéguet, Véronique ^a   Fiore, Christelle ^b   Schwimmer, Christine ^a   Dianoux, Anne Christine ^b   Vignais, Pierre V ^b   Brandolin, Gérard ^b   Lauquin, Guy J M ^a  

^a Institut de Biochimie et Genetique Cellulaires   (France)

^b CNRS   (France)

Author keywords

[No Author keywords available]

Indexed keywords

ADENINE NUCLEOTIDE TRANSLOCASE; ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATE; CYTOCHROME; ERGOSTEROL; MUTANT PROTEIN; TRYPTOPHAN;

ARTICLE; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; ENZYME ACTIVITY; FLUORESCENCE; LIGAND BINDING; MITOCHONDRION; NONHUMAN; NUCLEOTIDE TRANSPORT; PRIORITY JOURNAL; PROTEIN FOLDING; SACCHAROMYCES CEREVISIAE; SITE DIRECTED MUTAGENESIS;

ATRACTYLOSIDE; BASE SEQUENCE; BINDING SITES; DNA PRIMERS; ESCHERICHIA COLI; KINETICS; MITOCHONDRIA; MITOCHONDRIAL ADP, ATP TRANSLOCASES; MODELS, STRUCTURAL; MUTAGENESIS, SITE-DIRECTED; PLASMIDS; POINT MUTATION; PROTEIN CONFORMATION; PROTEIN STRUCTURE, SECONDARY; RECOMBINANT PROTEINS; SACCHAROMYCES CEREVISIAE; SPECTROMETRY, FLUORESCENCE; SPECTROPHOTOMETRY, ULTRAVIOLET; TRYPTOPHAN;

EID: 0030482902     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi961714i     Document Type: Article

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