Thermal stability and kinetic constants for 129 variants of a family 1 glycoside hydrolase reveal that enzyme activity and stability can be separately designed

Accurate modeling of enzyme activity and stability is an important goal of the protein engineering community. However, studies seeking to evaluate current progress are limited by small data sets of quantitative kinetic constants and thermal stability measurements. Here, we report quantitative measur...

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Veröffentlicht in:	PloS one 2017-05, Vol.12 (5), p.e0176255-e0176255
Hauptverfasser:	Carlin, Dylan Alexander, Hapig-Ward, Siena, Chan, Bill Wayne, Damrau, Natalie, Riley, Mary, Caster, Ryan W, Bethards, Bowen, Siegel, Justin B
Format:	Artikel
Sprache:	eng
Schlagworte:	Algorithms Amino acid sequence Antibiotic resistance Barnase Benchmarks Biocatalysts Biochemistry Biology and Life Sciences Catalysis Catalysts Catalytic Domain Cloning, Molecular Computer applications Computer programs Crystal structure Crystallography, X-Ray Datasets Design Directed evolution E coli Electrostatic properties Engineering Enzymatic activity Enzyme activity Enzyme kinetics Enzyme Stability Enzymes Escherichia coli Escherichia coli - enzymology Escherichia coli - genetics Gene mutation Genetic Variation Genetics Genomes Glycosidases Glycoside hydrolase Glycoside Hydrolases - chemistry Glycoside Hydrolases - genetics Glycosides Hydrolases Hydrolysis Immunogenicity Influenza Inhibitors Kinetics Learning algorithms Machinery Macromolecules Models, Molecular Molecular modelling Mutagenesis Mutants Mutation Optimization Peptides Physical Sciences Protein expression Protein Structure, Tertiary Proteins Public access Research and Analysis Methods Residues Statistical analysis Temperature Thermal stability
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