ArticleProtein science : a publication of the Protein Society2004
High-throughput automated refolding screening of inclusion bodies.
Article in Protein science : a publication of the Protein Society, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.
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41 citing papers in PubMed, 167 citations in OpenAlex.
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- Overcoming the Solubility Problem in E. coli: Available Approaches for Recombinant Protein Production.Methods in molecular biology (Clifton, N.J.) · 2022Review
- Identification of a Region in the Common Amino-terminal Domain of Hendra Virus P, V, and W Proteins Responsible for Phase Transition and Amyloid Formation.Biomolecules · 2021Article
- Advances in monitoring and control of refolding kinetics combining PAT and modeling.Applied microbiology and biotechnology · 2021Review
- Structural and Functional Characterization of the ABA-Water Deficit Stress Domain from Wheat and Barley: An Intrinsically Disordered Domain behind the Versatile Functions of the Plant Abscissic Acid, Stress and Ripening Protein Family.International journal of molecular sciences · 2021Article
- Biochemical characterization of a glycosyltransferase Gtf3 from3 Biotech · 2020Article
- Glutamic acid is a carrier for hydrazine during the biosyntheses of fosfazinomycin and kinamycin.Nature communications · 2018Article
- Downstream process development strategies for effective bioprocesses: Trends, progress, and combinatorial approaches.Engineering in life sciences · 2017Article
- Heterologous expression ofPeerJ · 2017Article
- Modulation of Re-initiation of Measles Virus Transcription at Intergenic Regions by PXD to NTAIL Binding Strength.PLoS pathogens · 2016Article
- DSF Guided Refolding As A Novel Method Of Protein Production.Scientific reports · 2016Article
- Approaches for the generation of active papain-like cysteine proteases from inclusion bodies of Escherichia coli.World journal of microbiology & biotechnology · 2015Review
- High throughput quantitative expression screening and purification applied to recombinant disulfide-rich venom proteins produced in E. coli.Journal of visualized experiments : JoVE · 2014Article
- Poly(ADP-ribose) polymerase is a substrate recognized by two metacaspases of Podospora anserina.Eukaryotic cell · 2013Article
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Authors and funding
10 authors at 2 institutions in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
One of the main stumbling blocks encountered when attempting to express foreign proteins in Escherichia coli is the occurrence of amorphous aggregates of misfolded proteins, called inclusion bodies (IB). Developing efficient protein native structure recovery procedures based on IB refolding is therefore an important challenge. Unfortunately, there is no "universal" refolding buffer: Experience shows that refolding buffer composition varies from one protein to another. In addition, the methods developed so far for finding a suitable refolding buffer suffer from a number of weaknesses. These include the small number of refolding formulations, which often leads to negative results, solubility assays incompatible with high-throughput, and experiment formatting not suitable for automation. To overcome these problems, it was proposed in the present study to address some of these limitations. This resulted in the first completely automated IB refolding screening procedure to be developed using a 96-well format. The 96 refolding buffers were obtained using a fractional factorial approach. The screening procedure is potentially applicable to any nonmembrane protein, and was validated with 24 proteins in the framework of two Structural Genomics projects. The tests used for this purpose included the use of quality control methods such as circular dichroism, dynamic light scattering, and crystallogenesis. Out of the 24 proteins, 17 remained soluble in at least one of the 96 refolding buffers, 15 passed large-scale purification tests, and five gave crystals.
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