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. 2016 Mar 17;7:10932. doi: 10.1038/ncomms10932

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The complex was produced by co-expression of the two proteins in the same cell. After affinity chromatography and gel filtration the tags were removed by thrombin cleavage followed by ion exchange chromatography. The fractions containing the complex were used for native PAGE and ES-MS. The ES-MS spectrum shows the presence of unfolded TIF2 (623–772) (poly-charged species), monomers of GR, monomer and dimer of GR bound to one molecule of TIF2. The transition from a poly-charged species of TIF2 to structured TIF2 when bound to GR indicates that the GR induces the folding of the co-activator molecule upon GR binding.