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![[Figure 3]](yt5053fig3mag.jpg)
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Figure 3
Thermodynamics of the TALE AvrBS3 binding to wild-type Bs3 and Bs3 A0, C0 and G0 target DNAs. (a) DNA sequence of the Bs3 DNA used in the fluorescence anisotropy and ITC binding assays (see also Supplementary Figs. S6 and S7). (b–e) DNA-binding profiles in the absence (solid circles) and the presence (open circles) of competitor DNA are depicted. The protein concentration [protein] has units of nM. The ITC assays show the nonlinear regression curve fitting of the data using a single-site binding model (solid circle) and a competitive binding model when the competitor DNA was present in the reaction (open circles). (f) The thermodynamic parameters of binding are reported. The obtained values are the average of four independent experiments. The KA of AvrBs3 association is shown for comparison purposes. Asterisks indicate the values of n, KA and ΔH obtained using a competitive-binding fitting model (see Supplementary Material). 1 cal = 4.186 J. |
![[Figure 3]](yt5053fig3.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
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