Relative tolerance of an enzymatic molten globule and its thermostable counterpart to point mutation

Biochemistry

Volumn 47, Issue 51, 2008, Pages 13489-13496

  Woycechowsky, Kenneth J ^a,b   Choutko, Alexandra ^a   Vamvaca, Katherina ^a,c   Hilvert, Donald ^a  

^a ETH ZURICH   (Switzerland)

^b UNIVERSITY OF UTAH   (United States)

^c HARVARD MEDICAL SCHOOL   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVE SITES; ACTIVITY LOSSES; ASPARTATE; BIOPHYSICAL CHARACTERIZATIONS; CATALYTIC ACTIVITIES; CATALYTIC EFFICIENCIES; CHORISMATE MUTASE; ENZYME STRUCTURES; FINE STRUCTURES; G VALUES; GLOBAL STABILITIES; HYDROPHOBIC CORES; MOLTEN GLOBULES; POINT MUTATIONS;

AMINES; AMINO ACIDS; CATALYSTS; ENZYMES; ORGANIC ACIDS; PLANTS (BOTANY); PROTEINS; SCAFFOLDS;

THERMODYNAMIC STABILITY;

AMINO ACID; CHORISMATE MUTASE; SCAFFOLD PROTEIN;

AMINO ACID SUBSTITUTION; ARTICLE; CATALYSIS; CHEMICAL ANALYSIS; CONTROLLED STUDY; DNA SEQUENCE; ENZYME ACTIVE SITE; ENZYME STRUCTURE; HYDROPHOBICITY; POINT MUTATION; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN SECONDARY STRUCTURE; THERMOSTABILITY;

CATALYSIS; CATALYTIC DOMAIN; CHORISMATE MUTASE; CIRCULAR DICHROISM; METHANOCOCCUS; MOLECULAR CONFORMATION; MUTATION; PHENYLALANINE; POINT MUTATION; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; THERMODYNAMICS; TRYPTOPHAN;

EID: 58149165033     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi801108a     Document Type: Article

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