ArticleNature communications2016
Connecting two proteins using a fusion alpha helix stabilized by a chemical cross linker.
Article in Nature communications, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed.
- Backbone rigidity of disordered protein linkers from NMR experiments and MD simulations.Biophysical journal · 2026Article
- Thyme, Oregano, and Cinnamon Essential Oils: Investigating Their Molecular Mechanism of Action for the Treatment of Bacteria-Induced Cystitis.ACS omega · 2026Article
- HIV Membrane-Proximal External Region Scaffolded Immunogen as Killed Whole-Cell Genome-Reduced Vaccines.Viruses · 2026Article
- Article
- Structural determination of small proteins by cryo-EM using a coiled coil module strategy.Scientific reports · 2025Article
- Editorial: Fusion proteins for the detection of pathogens or pathogen receptors.Frontiers in bioengineering and biotechnology · 2025Article
- Mitigating the Blurring Effect of CryoEM Averaging on a Flexible and Highly Symmetric Protein Complex through Sub-Particle Reconstruction.International journal of molecular sciences · 2024Article
- Programming interchangeable and reversible heterooligomeric protein self-assembly using a bifunctional ligand.Chemical science · 2024Article
- Protein Stability: Enhancement and Measurement.Methods in molecular biology (Clifton, N.J.) · 2023Article
- Article
- Development of imaging scaffolds for cryo-electron microscopy.Current opinion in structural biology · 2020Review
- Fusion of DARPin to Aldolase Enables Visualization of Small Protein by Cryo-EM.Structure (London, England : 1993) · 2019Article
- Construction of novel repeat proteins with rigid and predictable structures using a shared helix method.Scientific reports · 2017Article
- Fusion to a homo-oligomeric scaffold allows cryo-EM analysis of a small protein.Scientific reports · 2016Article
Corrections and comments
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Authors and funding
8 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Building a sophisticated protein nano-assembly requires a method for linking protein components in a predictable and stable structure. Most of the cross linkers available have flexible spacers. Because of this, the linked hybrids have significant structural flexibility and the relative structure between their two components is largely unpredictable. Here we describe a method of connecting two proteins via a 'fusion α helix' formed by joining two pre-existing helices into a single extended helix. Because simple ligation of two helices does not guarantee the formation of a continuous helix, we used EY-CBS, a synthetic cross linker that has been shown to react selectively with cysteines in α-helices, to stabilize the connecting helix. Formation and stabilization of the fusion helix was confirmed by determining the crystal structures of the fusion proteins with and without bound EY-CBS. Our method should be widely applicable for linking protein building blocks to generate predictable structures.
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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 OpenQuestion graph.