Features of F1-ATPase catalytic and noncatalytic sites revealed by fluorescence lifetimes and acrylamide quenching of specifically inserted tryptophan residues

Biochemistry

Volumn 39, Issue 18, 2000, Pages 5287-5294

  Weber, Joachim ^a   Senior, Alan E ^a  

^a UNIVERSITY OF ROCHESTER MEDICAL CENTER   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ACRYLAMIDE; MAGNESIUM ION; NUCLEOTIDE; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATE SYNTHASE; TRYPTOPHAN;

ARTICLE; CRYSTAL STRUCTURE; ENZYME ACTIVE SITE; ENZYME ANALYSIS; ENZYME CONFORMATION; ENZYME STRUCTURE; ESCHERICHIA COLI; FLUORESCENCE; NONHUMAN; PRIORITY JOURNAL; PROTEIN BINDING; STRUCTURE ANALYSIS;

ACRYLAMIDE; BINDING SITES; ESCHERICHIA COLI; KINETICS; MAGNESIUM; MODELS, MOLECULAR; MUTATION; NUCLEOTIDES; PROTEIN BINDING; PROTEIN CONFORMATION; PROTON-TRANSLOCATING ATPASES; SPECTROMETRY, FLUORESCENCE; TRYPTOPHAN;

ESCHERICHIA COLI; NEGIBACTERIA;

EID: 0034625038     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi992730t     Document Type: Article

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