Intrinsic fluorescence studies of the chaperonin GroEL containing single Tyr → Trp replacements reveal ligand-induced conformational changes

Journal of Biological Chemistry

Volumn 271, Issue 50, 1996, Pages 31989-31995

  Gibbons, Don L ^a,c   Hixson, John D ^a   Hay, Nicki ^b   Lund, Peter ^b   Gorovits, Boris M ^a   Ybarra, Jesse ^a   Horowitz, Paul M ^a  

^a Mays Cancer Center at UT Health San Antonio   (United States)

^b UNIVERSITY OF BIRMINGHAM   (United Kingdom)

^c ALBERT EINSTEIN COLLEGE OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE DIPHOSPHATE; ADENYLYLIMIDODIPHOSPHATE; CHAPERONIN; MUTANT PROTEIN; NUCLEOTIDE; THIOSULFATE SULFURTRANSFERASE; TRYPTOPHAN; TYROSINE; UREA;

AMINO ACID SUBSTITUTION; ARTICLE; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; ENERGY TRANSFER; FLUORESCENCE; HYDROPHOBICITY; NONHUMAN; PRIORITY JOURNAL; PROTEIN ASSEMBLY; PROTEIN BINDING; PROTEIN FOLDING; PROTEIN PURIFICATION; PROTEIN QUATERNARY STRUCTURE;

ADENOSINE DIPHOSPHATE; ADENYLYL IMIDODIPHOSPHATE; GROEL PROTEIN; MAGNESIUM; MUTAGENESIS, SITE-DIRECTED; POTASSIUM; PROTEIN CONFORMATION; SPECTROMETRY, FLUORESCENCE; TRYPTOPHAN; TYROSINE;

EID: 0029731414     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.271.50.31989     Document Type: Article

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