ArticleInternational journal of molecular sciences2021
Rational Design of Adenylate Kinase Thermostability through Coevolution and Sequence Divergence Analysis.
Article in International journal of molecular sciences, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 9 citations in OpenAlex.
- Thermostability Engineering in Therapeutic Antioxidant Enzymes: From Molecular Fundamentals to Oxidative Stress Applications.International journal of molecular sciences · 2026Review
- Computer-aided engineering of stabilized fibroblast growth factor 21.Computational and structural biotechnology journal · 2024Article
- Identifying the minimal sets of distance restraints for FRET-assisted protein structural modeling.Protein science : a publication of the Protein Society · 2024Article
- Identifying the minimal sets of distance restraints for FRET-assisted protein structural modeling.ArXiv · 2024Article
- Understanding the Stabilization Mechanism of a Thermostable Mutant of Hygromycin B Phosphotransferase by Protein Sector-Guided Dynamic Analysis.ACS omega · 2023Article
- DeepTM: A deep learning algorithm for prediction of melting temperature of thermophilic proteins directly from sequences.Computational and structural biotechnology journal · 2023Article
- Special Issue on "Enzymes as Biocatalysts: Current Research Trends and Applications".International journal of molecular sciences · 2022Article
- Therapeutic enzyme engineering using a generative neural network.Scientific reports · 2022Article
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Authors and funding
4 authors at 1 institution in 2 countries.
Funding
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
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Registered trials
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