ArticlePLoS computational biology2015
FireProt: Energy- and Evolution-Based Computational Design of Thermostable Multiple-Point Mutants.
Article in PLoS computational biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 72 papers.
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Who cites it
72 citing papers in PubMed.
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- Improved biosynthesis of lactulose by a novel thermostable cellobiose-2-epimerase generated through semi-rational mutagenesis.World journal of microbiology & biotechnology · 2025Article
- Network Dynamics as Fingerprints of Thermostability in an In Silico-Engineered DyP-Type Peroxidase.ACS catalysis · 2025Article
- Decoding Protein Stabilization: Impact on Aggregation, Solubility, and Unfolding Mechanisms.Journal of chemical information and modeling · 2025Article
- GArNet: A Genetic Algorithm-Based Protein Redesign Approach to Optimize Mutation Combinations Informed by Network Theory.Journal of chemical information and modeling · 2025Article
- Increased thermal stability of FGF10 leads to ectopic signaling during development.Cellular and molecular life sciences : CMLS · 2025Article
- Improvement in the Thermal Stability ofMolecules (Basel, Switzerland) · 2025Article
- FoldX force field revisited, an improved version.Bioinformatics (Oxford, England) · 2025Article
- A Practical Guide to Computational Tools for Engineering Biocatalytic Properties.International journal of molecular sciences · 2025Review
- Structure-based self-supervised learning enables ultrafast protein stability prediction upon mutation.Innovation (Cambridge (Mass.)) · 2025Article
- Multiple strategies were adopted to optimize the enzymatic characteristics and improve the expression of bovine chymosin BtChy inFrontiers in microbiology · 2025Article
- Computer-Aided Design to Improve the Thermal Stability ofFoods (Basel, Switzerland) · 2024Article
- Enhancement of the Thermostability ofMolecules (Basel, Switzerland) · 2024Article
- GRAPE-WEB: An automated computational redesign web server for improving protein thermostability.mLife · 2024Article
- Computer-aided engineering of stabilized fibroblast growth factor 21.Computational and structural biotechnology journal · 2024Article
- Structural analysis of the stable form of fibroblast growth factor 2 - FGF2-STAB.Journal of structural biology: X · 2024Article
- Opportunities and challenges in design and optimization of protein function.Nature reviews. Molecular cell biology · 2024Review
- Biosynthetic production of anticoagulant heparin polysaccharides through metabolic and sulfotransferases engineering strategies.Nature communications · 2024Article
- Thermostability Enhancement of GH 62 α-l-Arabinofuranosidase by Directed Evolution and Rational Design.Journal of agricultural and food chemistry · 2024Article
12 more citing papers are in PubMed but not listed here.
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Authors and funding
10 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
There is great interest in increasing proteins' stability to enhance their utility as biocatalysts, therapeutics, diagnostics and nanomaterials. Directed evolution is a powerful, but experimentally strenuous approach. Computational methods offer attractive alternatives. However, due to the limited reliability of predictions and potentially antagonistic effects of substitutions, only single-point mutations are usually predicted in silico, experimentally verified and then recombined in multiple-point mutants. Thus, substantial screening is still required. Here we present FireProt, a robust computational strategy for predicting highly stable multiple-point mutants that combines energy- and evolution-based approaches with smart filtering to identify additive stabilizing mutations. FireProt's reliability and applicability was demonstrated by validating its predictions against 656 mutations from the ProTherm database. We demonstrate that thermostability of the model enzymes haloalkane dehalogenase DhaA and γ-hexachlorocyclohexane dehydrochlorinase LinA can be substantially increased (ΔTm = 24°C and 21°C) by constructing and characterizing only a handful of multiple-point mutants. FireProt can be applied to any protein for which a tertiary structure and homologous sequences are available, and will facilitate the rapid development of robust proteins for biomedical and biotechnological applications.
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