ArticleProtein science : a publication of the Protein Society2004
An automated in vitro protein folding screen applied to a human dynactin subunit.
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 14 papers.
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14 citing papers in PubMed, 39 citations in OpenAlex.
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- Methyl group assignment using pseudocontact shifts with PARAssign.Journal of biomolecular NMR · 2017Article
- Structural Basis of Cyclic Nucleotide Selectivity in cGMP-dependent Protein Kinase II.The Journal of biological chemistry · 2016Article
- DSF Guided Refolding As A Novel Method Of Protein Production.Scientific reports · 2016Article
- TraG encoded by the pIP501 type IV secretion system is a two-domain peptidoglycan-degrading enzyme essential for conjugative transfer.Journal of bacteriology · 2013Article
- Green fluorescent protein-labeled monitoring tool to quantify conjugative plasmid transfer between Gram-positive and Gram-negative bacteria.Applied and environmental microbiology · 2012Article
- Experimental optimization of protein refolding with a genetic algorithm.Protein science : a publication of the Protein Society · 2010Article
- Dynamitin mutagenesis reveals protein-protein interactions important for dynactin structure.Traffic (Copenhagen, Denmark) · 2008Article
- Refolding of a membrane protein in a microfluidics reactor.European biophysics journal : EBJ · 2007Article
- A type IV-secretion-like system is required for conjugative DNA transport of broad-host-range plasmid pIP501 in gram-positive bacteria.Journal of bacteriology · 2007Article
- Article
- Investigation of protein refolding using a fractional factorial screen: a study of reagent effects and interactions.Protein science : a publication of the Protein Society · 2005Article
- High-throughput automated refolding screening of inclusion bodies.Protein science : a publication of the Protein Society · 2004Article
- Fast identification of folded human protein domains expressed in E. coli suitable for structural analysis.BMC structural biology · 2004Article
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Authors and funding
4 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The preparation of proteins for structural and functional analysis using the Escherichia coli expression system is often hampered by the formation of insoluble intracellular protein aggregates (inclusion bodies). Transferring those proteins into their native states by in vitro protein folding requires screening for the best buffer conditions and suitable additives. However, it is difficult to assess the success of such a screen if no biological assay is available. We established a fully automated folding screen and a system to detect folded protein that is based on analytical hydrophobic interaction chromatography and tryptophan fluorescence spectroscopy. The system was evaluated with two model enzymes (carbonic anhydrase II and malate dehydrogenase), and was successfully applied to the folding of the p22 subunit of human dynactin, which is expressed in inclusion bodies in E. coli. The described screen allows for high-throughput folding analysis of inclusion body proteins for structural and functional analyses.
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