Figure 3
From: Protein expression, characterization and activity comparisons of wild type and mutant DUSP5 proteins
Protein characterization. (A) Mass spectrometric analysis was performed by Bioproximity, LLC on coomassie identified bands of the appropriate size separated by SDS-PAGE. Samples were subjected to in-gel trypsin digestion and the peptides recovered for mass spectrometric analysis. (B) Circular dichroism was performed to determine folding and secondary structure of DUSP5, which was found to be 43% alpha helical and 20% beta-sheet. (C) Dynamic Light Scattering predicts oligomerization of both DUSP5 and S147P. (D & E) GST-DUSP5 is active and sensitive to the addition of DTT. Specifically, 1Â mM DTT increased the activity of GST-DUSP5 against pERK2 in vitro.