ArticleCommunications biology2021
Synergistic stabilization of a double mutant in chymotrypsin inhibitor 2 from a library screen in E. coli.
Article in Communications biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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.
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Who cites it
7 citing papers in PubMed, 23 citations in OpenAlex.
- Residue-Specific Signatures of Structural Water Identified by Dissolution Dynamic Nuclear Polarization with UV-Generated Radicals.Angewandte Chemie (International ed. in English) · 2026Article
- Protein stability models fail to capture epistatic interactions of double point mutations.Protein science : a publication of the Protein Society · 2025Article
- Design of a novel chimeric peptide via dual blockade of CD47/SIRPα and PD-1/PD-L1 for cancer immunotherapy.Science China. Life sciences · 2023Article
- Slow conformational changes in the rigid and highly stable chymotrypsin inhibitor 2.Protein science : a publication of the Protein Society · 2023Article
- Accurate protein stability predictions from homology models.Computational and structural biotechnology journal · 2023Article
- Increasing protein stability by inferring substitution effects from high-throughput experiments.Cell reports methods · 2022Article
- A dual-reporter system for investigating and optimizing protein translation and folding in E. coli.Nature communications · 2021Article
Corrections and comments
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Most single point mutations destabilize folded proteins. Mutations that stabilize a protein typically only have a small effect and multiple mutations are often needed to substantially increase the stability. Multiple point mutations may act synergistically on the stability, and it is often not straightforward to predict their combined effect from the individual contributions. Here, we have applied an efficient in-cell assay in E. coli to select variants of the barley chymotrypsin inhibitor 2 with increased stability. We find two variants that are more than 3.8 kJ mol
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Registered trials
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