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. Author manuscript; available in PMC: 2011 Nov 30.
Published in final edited form as: Biochemistry. 2011 Jul 13;50(32):6920–6932. doi: 10.1021/bi200498q

Figure 3.

Figure 3

Guanidine hydrochloride denaturation of sc-S100A4 proteins. (A) Unfolding of 5 μM wild-type S100A4 dimer or sc-S100A4 proteins in the presence of 2 mM EGTA. wt-S100A4, sc-S100A4–5, and sc-S100A4–10 exhibited similar midpoints of denaturation. (B) Unfolding in the presence of 2 mM CaCl2. The sc-S100A4 proteins were more resistant to denaturant-induced unfolding than wt-S100A4. wt-S100A4 (black), sc-S100A4–5 (red), and sc-S100A4–10 (blue). Values represent the mean ± standard error of the mean from three or four independent experiments.