ArticleAngewandte Chemie (International ed. in English)2022
Design of a Protein with Improved Thermal Stability by an Evolution-Based Generative Model.
Article in Angewandte Chemie (International ed. in English), 2022. 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, 14 citations in OpenAlex.
- Protein stability is determined by single-site bias rather than pairwise covariance.Nature chemical biology · 2026Article
- Generative Landscapes and Dynamics to Design Functional Multidomain Artificial Transmembrane Transporters.ACS central science · 2025Article
- A Cyanobacterial Screening Platform for Rubisco Mutant Variants.ACS synthetic biology · 2025Article
- Quaternary stabilization of a GH2 β-galactosidase from the psychrophile A. ikkensis, a flexible and unstable dimeric enzyme.Protein science : a publication of the Protein Society · 2025Article
- Computational scoring and experimental evaluation of enzymes generated by neural networks.Nature biotechnology · 2025Article
- PROSCA: an online platform for humanized scaffold mining facilitating rational protein engineering.Nucleic acids research · 2024Article
- In vivo functional phenotypes from a computational epistatic model of evolution.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Design of a Protein with Improved Thermal Stability by an Evolution-Based Generative Model.Angewandte Chemie (International ed. in English) · 2022Article
Corrections and comments
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Authors and funding
11 authors at 6 institutions in 4 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Efficient design of functional proteins with higher thermal stability remains challenging especially for highly diverse sequence variants. Considering the evolutionary pressure on protein folds, sequence design optimizing evolutionary fitness could help designing folds with higher stability. Using a generative evolution fitness model trained to capture variation patterns in natural sequences, we designed artificial sequences of a proteinaceous inhibitor of pectin methylesterase enzymes. These inhibitors have considerable industrial interest to avoid phase separation in fruit juice manufacturing or reduce methanol in distillates, averting chromatographic passages triggering unwanted aroma loss. Six out of seven designs with up to 30 % divergence to other inhibitor sequences are functional and two have improved thermal stability. This method can improve protein stability expanding functional protein sequence space, with traits valuable for industrial applications and scientific research.
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