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. Author manuscript; available in PMC: 2017 Jan 17.
Published in final edited form as: Biochemistry. 2015 Sep 17;54(38):5949–5958. doi: 10.1021/acs.biochem.5b00678

Figure 2.

Figure 2

Binding profiles of αA-crystallins to destabilized T4L mutants. An increase in α-crystallin binding affinity and/or capacity is observed with a progressive decrease in T4L stability, which is reported as a left-shift in the data. Whereas the binding pattern of human (A) and zebrafish (B) αA are comparable, rat αAins (C) shows substantial enhancement of activity. Solid lines are the non-linear least squares fits of the curves and the parameters are reported in Table 3. All binding curves were generated in pH 7.2 buffer at 37 °C.