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• W3135370424 abstract "Protein engineering is actively pursued in industrial and laboratory settings for high thermostability. Among the many protein engineering methods, rational design by bioinformatics provides theoretical guidance without time-consuming experimental screenings. However, most rational design methods either rely on protein tertiary structure information or have limited accuracies. We proposed a primary-sequence-based algorithm for increasing the heat resistance of a protein while maintaining its functions. Using adenylate kinase (ADK) family as a model system, this method identified a series of amino acid sites closely related to thermostability. Single- and double-point mutants constructed based on this method increase the thermal denaturation temperature of the mesophilic Escherichia coli (E. coli) ADK by 5.5 and 8.3 °C, respectively, while preserving most of the catalytic function at ambient temperatures. Additionally, the constructed mutants have improved enzymatic activity at higher temperature." @default.
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• W3135370424 date "2021-03-09" @default.
• W3135370424 modified "2023-10-17" @default.
• W3135370424 title "Rational Design of Adenylate Kinase Thermostability through Coevolution and Sequence Divergence Analysis" @default.
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• W3135370424 doi "https://doi.org/10.3390/ijms22052768" @default.
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