ArticleProtein science : a publication of the Protein Society2026
Use of tandem-affinity chromatography to incorporate nucleotide loading of small GTPases during their purification.
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.
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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
1 citing paper in PubMed.
- Use of tandem-affinity chromatography to incorporate nucleotide loading of small GTPases during their purification.Protein science : a publication of the Protein Society · 2026Article
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Authors and funding
5 authors.
Funding
Abstract
A bottleneck for structure-function studies of closely related proteins is purification. Here, we built upon new affinity protein purification technology to develop a uniform and rapid tandem-affinity purification protocol to generate significant quantities of pure GTPase proteins for use in structure-function studies. Our method relies on new and commercially available split-intein based technology. We show that this technology can be used to speed up purification of small GTPases and at the same time facilitate nucleotide loading. Using K-Ras4B and H-Ras as case studies, we demonstrate that we can generate crystallizable grade protein, homogenously loaded with either GDP or the non-hydrolysable GTP analogue GppNHp, in less than 36 h.
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Registered trials
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