Time-resolved fluorescence anisotropy study of the refolding reaction of the α-subunit of tryptophan synthase reveals nonmonotonic behavior of the rotational correlation time

Biochemistry

Volumn 38, Issue 13, 1999, Pages 4177-4187

  Bilsel, Osman ^a   Yang, Li ^b,c   Zitzewitz, Jill A ^a   Beechem, Joseph M ^b   Matthews, C Robert ^a  

^a PENNSYLVANIA STATE UNIVERSITY   (United States)

^b VANDERBILT UNIVERSITY SCHOOL OF MEDICINE   (United States)

^c Laboratory of Atomic and Solid State Physics and Sibley School of Mechanical and Aerospace Engineering   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

TRYPTOPHAN SYNTHASE;

ALPHA CHAIN; AMINO ACID COMPOSITION; AMINO TERMINAL SEQUENCE; ANISOTROPY; ARTICLE; CARBOXY TERMINAL SEQUENCE; ESCHERICHIA COLI; FLUORESCENCE ANALYSIS; NONHUMAN; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN INTERACTION; PROTEIN STRUCTURE; REACTION ANALYSIS;

ANILINO NAPHTHALENESULFONATES; ESCHERICHIA COLI; FLUORESCENCE POLARIZATION; KINETICS; MODELS, CHEMICAL; PROTEIN FOLDING; SPECTROMETRY, FLUORESCENCE; TIME FACTORS; TRYPTOPHAN SYNTHASE; TYROSINE;

EID: 0033616632     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi9829433     Document Type: Article

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