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. Author manuscript; available in PMC: 2017 Nov 1.
Published in final edited form as: Structure. 2016 Sep 22;24(11):1898–1906. doi: 10.1016/j.str.2016.08.011

Figure 2. T2D stabilizes the native state of SOD1 through decreased dimer dissociation rates.

Figure 2

(A) Size exclusion chromatograms showing the populations of native dimer (15.5 ml) and monomer (17.4 ml) for unmodified T2D-, T2D/A4V- and WT-SOD1. Samples were taken after incubation at physiological conditions (30 µM SOD1, pH 7.4) and 37°C for 7 days. (B) Size exclusion chromatograms for glutathionylated T2D-, T2D/A4V- and WT-SOD1. Dissociation of immobilized dimers was monitored by surface plasmon resonance for T2D-, T2D/A4V- and WT-SOD1 (C) and glutathionylated species (D). Thermal denaturation curves of unmodified (E) and glutathionylated(F) SOD1 proteins indicate the Tm of T2D-SOD1 is lower than that of WT-SOD1 in the unfolding of SOD1 monomers. Fitting to a two-state model is represented as lines. Size exclusion chromatograms, dissociation profile and thermal denaturation curves of A4V–SOD1 and GS-A4V–SOD1 have been reported (Redler et al., 2011). See also Figure S4.