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. Author manuscript; available in PMC: 2013 Feb 17.
Published in final edited form as: J Mol Biol. 2011 Dec 21;416(2):208–220. doi: 10.1016/j.jmb.2011.12.030

Figure 2. Differential scanning fluorimetry traces showing the effect of the disulfide bond, pH, and D236A mutation on the thermal stability of ArfA.

Figure 2

(a–c) Protein was treated with DTT or GSSG to break or form the C208–C250 disulfide bond. ArfA-b1 encompasses residues 73 to 220. (d) Traces were obtained for wild-type ArfA-c at pH7 (black) or pH4 (orange) and for ArfA-c(D236A) at pH7 (cyan).