ArticleProtein science : a publication of the Protein Society2019
Translation-coupled protein folding assay using a protease to monitor the folding status.
Article in Protein science : a publication of the Protein Society, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 12 citations in OpenAlex.
- High-throughput Selection of Human de novo-emerged sORFs with High Folding Potential.Genome biology and evolution · 2024Article
- Mapping Protein-Protein Interactions at Birth: Single-Particle Cryo-EM Analysis of a Ribosome-Nascent Globin Complex.ACS central science · 2024Article
- Experimental characterization of de novo proteins and their unevolved random-sequence counterparts.Nature ecology & evolution · 2023Article
- Modern and prebiotic amino acids support distinct structural profiles in proteins.Open biology · 2022Article
- In Vitro Evolution Reveals Noncationic Protein-RNA Interaction Mediated by Metal Ions.Molecular biology and evolution · 2022Article
- Protein Science Best Paper awards to Tatsuya Niwa, Qingping Xu, and Matthew Biancalana.Protein science : a publication of the Protein Society · 2020Article
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4 authors at 1 institution in 1 country.
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Abstract
Protein folding is an essential prerequisite for proteins to execute nearly all cellular functions. There is a growing demand for a simple and robust method to investigate protein folding on a large-scale under the same conditions. We previously developed a global folding assay system, in which proteins translated using an Escherichia coli-based cell-free translation system are centrifuged to quantitate the supernatant fractions. Although the assay is based on the assumption that the supernatants contain the folded native states, the supernatants also include nonnative unstructured proteins. In general, proteases recognize and degrade unstructured proteins, and thus we used a protease to digest the unstructured regions to monitor the folding status. The addition of Lon protease during the translation of proteins unmasked subfractions, not only in the soluble fractions but also in the aggregation-prone fractions. We translated ∼90 E. coli proteins in the protease-inclusion assay, in the absence and presence of chaperones. The folding assay, which sheds light on the molecular mechanisms underlying the aggregate formation and the chaperone effects, can be applied to a large-scale analysis.
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