ArticleProtein science : a publication of the Protein Society2008
NMR spectroscopy as a tool for the rapid assessment of the conformation of GST-fusion proteins.
Article in Protein science : a publication of the Protein Society, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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4 citing papers in PubMed.
- Expansion of GA Dinucleotide Repeats Increases the Density of CLAMP Binding Sites on the X-Chromosome to Promote Drosophila Dosage Compensation.PLoS genetics · 2016Article
- ATM-mediated phosphorylation of SOG1 is essential for the DNA damage response in Arabidopsis.EMBO reports · 2013Article
- A structural basis for the regulation of the LIM-homeodomain protein islet 1 (Isl1) by intra- and intermolecular interactions.The Journal of biological chemistry · 2013Article
- Efficient protein production method for NMR using soluble protein tags with cold shock expression vector.Journal of biomolecular NMR · 2010Article
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4 authors.
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Abstract
Glutathione-S-transferase (GST)-fusion proteins are used extensively for structural, biochemical, and functional analyses. Although the conformation of the target protein is of critical importance, confirmation of the folded state of the target is often not undertaken or is cumbersome because of the requirement to first remove the GST tag. Here, we demonstrate that it is possible to record conventional (15)N-HSQC NMR spectra of small GST-fusion proteins and that the observed signals arise almost exclusively from the target protein. This approach constitutes a rapid and straightforward means of assessing the conformation of a GST-fusion protein without having to cleave the GST and should prove valuable, both to biochemists seeking to check the conformation of their proteins prior to functional studies and to structural biologists screening protein constructs for suitability as targets for structural studies.
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