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. Author manuscript; available in PMC: 2019 Feb 9.
Published in final edited form as: Biochemistry. 2016 May 4;55(19):2794–2805. doi: 10.1021/acs.biochem.6b00006

Figure 5.

Figure 5.

Assessment of the relative thermostability of purified Purβ point mutants. (A) The unfolding of wild-type (WT) Purβ in comparison to point mutants R267A (single), R159A/R267A (double), and K82A/R159A/R267A (triple) was evaulated by thermal shift assay at a protein concentration of 2.8 μM in 50 mM sodium phosphate pH 8.0, 300 mM NaCl, 10 mM imidazole, 10 mM β-mercaptoethanol. (B) Bars show the calculated Tm of each protein determined at multiple protein concentrations ranging from 1.0 to 8.5 μM (mean ± SD, n = 6–10).