Structural perturbation and compensation by directed evolution at physiological temperature leads to thermostabilization of β-lactamase

Biochemistry

Volumn 44, Issue 38, 2005, Pages 12640-12654

  Hecky, Jochen ^a   Müller, Kristian M ^a  

^a UNIVERSITY OF FREIBURG   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

ANTIBIOTICS; LOW TEMPERATURE EFFECTS; METABOLISM; OPTIMIZATION; PERTURBATION TECHNIQUES;

DESTABILIZATION; PATHOGENS; THERMOACTIVITY; TIME RESOLVED KINETICS;

ENZYMES;

ALANINE; BETA LACTAM ANTIBIOTIC; BETA LACTAMASE; METHIONINE; THREONINE; VALINE;

AMINO TERMINAL SEQUENCE; ANTIBIOTIC RESISTANCE; ARTICLE; CONTROLLED STUDY; DELETION MUTANT; DNA SHUFFLING; ENZYME ACTIVITY; ENZYME ASSAY; ENZYME DENATURATION; ENZYME KINETICS; ENZYME STABILITY; ENZYME STRUCTURE; EVOLUTION; HALF LIFE TIME; MUTAGENESIS; PRIORITY JOURNAL; PROTEIN FOLDING; THERMODYNAMICS; THERMOSTABILITY;

AMINO ACID SEQUENCE; BETA-LACTAMASES; CATALYSIS; DIRECTED MOLECULAR EVOLUTION; ENZYME STABILITY; KINETICS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PROTEIN DENATURATION; SEQUENCE DELETION; TEMPERATURE;

EID: 25444463283     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi0501885     Document Type: Article

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