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. 2014 Dec 18;15:27. doi: 10.1186/s12858-014-0027-0

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© Nayak et al.; licensee BioMed Central. 2014

This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly credited. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated.

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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, 1 mM DTT increased the activity of GST-DUSP5 against pERK2 in vitro.