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. 2006 May;15(5):1193–1198. doi: 10.1110/ps.062092506

Figure 4.

Figure 4.

 Thermodynamic stability and binding activity of the TPR domain of UBP. (A) Far-UV CD spectrum of the TPR domain of UBP (residues 88–208) at 12 μM protein concentration in 150 mM NaCl, 50 mM phosphate buffer (pH 6.5) at 25°C. (B) Thermal denaturation curve of UBP TPR domain monitored by the change in ellipticity signal at 222 nm as described in Figure 2. (C) Binding activity of UBP TPR domain to C-terminal 24-mer peptide of Hsp70 measured by SPR. The response at the equilibrium data at increasing protein concentration was fit to a one-site saturation model to calculate the dissociation binding constant (KD UBP-TPR/Hsp70 = 225 μM).