Tryptophan phosphorescence study of enzyme flexibility and unfolding in laboratory-evolved thermostable esterases

Biochemistry

Volumn 39, Issue 16, 2000, Pages 4658-4665

  Gershenson, Anne ^a   Schauerte, Joseph A ^b   Giver, Lori ^a,c   Arnold, Frances H ^a  

^a California Institute of Technology   (United States)

^b UNIVERSITY OF MICHIGAN HEALTH SYSTEM   (United States)

^c MAXYGEN INC   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ESTERASE;

ARTICLE; ENZYME CONFORMATION; ENZYME STABILITY; ESCHERICHIA COLI; MOLECULAR INTERACTION; NONHUMAN; PHOSPHORESCENCE; PRIORITY JOURNAL; THERMOSTABILITY;

DIRECTED MOLECULAR EVOLUTION; DITHIONITROBENZOIC ACID; ENZYME STABILITY; ESTERASES; HYDROGEN-ION CONCENTRATION; HYDROLYSIS; KINETICS; LUMINESCENT MEASUREMENTS; MODELS, MOLECULAR; MUTATION; NITROPHENOLS; PLIABILITY; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; TEMPERATURE; TRYPTOPHAN; VIBRATION;

ESCHERICHIA COLI;

EID: 0034712678     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi992473s     Document Type: Article

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