ArticleProtein science : a publication of the Protein Society2026
Disordered N-termini enhance the thermostability of SGNH-hydrolase family polyesterases.
Article in Protein science : a publication of the Protein Society, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
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Who cites it
1 citing paper in PubMed.
- Disordered N-termini enhance the thermostability of SGNH-hydrolase family polyesterases.Protein science : a publication of the Protein Society · 2026Article
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Authors and funding
8 authors.
Funding
Abstract
Polyesters are widely used plastics that persist in the environment due to their resistance to degradation. Microbial polyesterases potentially offer recycling and remediation solutions. However, most polyesterases lack the thermostability and catalytic efficiency required for practical application. Here, we have identified and characterized thermostable bacterial polyesterases from an undercharacterized subfamily of SGNH-hydrolases (related to PpEST from Pseudomonas oleovorans) and uncovered a previously unreported thermal stabilization mechanism mediated by conformationally flexible N-terminal regions with features of intrinsically disordered regions. Biochemical assays, structural analysis, small angle X-ray scattering, X-ray crystallography, and molecular dynamics simulations suggest that these flexible N-terminal regions enhance thermal resilience without affecting the catalytic rate or oligomerization in some homologs, while they promote oligomerization and reduce k
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the Socratic graph.