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Φ-value analysis of the unfolding data revealed a highly native transition state.

The expression depending on the equilibrium unfolding data from multimeric proteins that have a two-state monomer.

The temperature-dependent unfolding data were analyzed as previously described [11].

The results obtained from our native PAGE analysis of thermal unfolding were in good agreement with the CD thermal unfolding data.

This mutant enzyme also had less than 20% activity at 70°C (Figure 3C), consistent with the CD thermal unfolding data.

It should be noted that the results obtained from native PAGE analysis of thermal unfolding were found to be in good agreement with the CD thermal unfolding data, as well as the profiles of thermal inactivation of xylanase activity.

Figure 3 also shows the GdnHCl-induced unfolding data for Tk-RNase HII and Ec-RNase HI.

Folding and unfolding data (as Arrhenius plots) for [P18A]-TC16b [P18A]-TC16b8andTC16b at pH 2.5, and [P17A,P18A]-TC16b at pH 7.

To investigate this hypothesis, empirical unfolding data from Toolkit peptides at different stages of purification was collected.

The CD unfolding data highlight the marked instability of the coiled-coil structure to decreases in pH.

Moreover, thermal unfolding data (Fig. 3b) showed an unfolding transition at slightly higher temperatures for the dual cysteine mutants, indicating that, if anything, the N36C, D105C mutations may increase the stability of HER2DARPin.