Urea Unfolding Study of E. coli Alanyl-tRNA Synthetase and Its Monomeric Variants Proves the Role of C-Terminal Domain in Stability

Figure 2

Unfolding profile of WT-alaRS (a), G674D (b), N700 alaRS (c), and N461 (d). The graph was made by plotting the fluorescence intensity ratio change (/) and alterations in emission maximum with increasing urea concentration. All the protein concentrations were kept at 4 μM. Samples were excited at 295 nm where excitation and emission bandpasses were kept as 5 nm for both. A circulating water bath was used to maintain the temperature at 25°C. The buffer was 100 mM Tris-HCl, pH 8.0.

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