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. Author manuscript; available in PMC: 2009 Aug 1.
Published in final edited form as: Biochimie. 2008 Apr 4;90(8):1233–1249. doi: 10.1016/j.biochi.2008.03.011

Table 3.

Temperature Dependence of the ITC-Derived Parameters for the Binding of HXDV and HXLV-AC to hTel24-NMR in the presence of 50 mM K+a

Compound Temperature (°C) K (M−1) ΔH (kcal/mol) N
HXDV 25 (3.0 ± 0.4) × 105 −1.7 ± 0.1 2.2 ± 0.1
HXDV 30 (2.8 ± 0.4) × 105 −2.4 ± 0.1 2.0 ± 0.1
HXDV 35 (3.5 ± 0.3) × 105 −3.1 ± 0.1 1.9 ± 0.1
HXDV 40 (6.9 ± 0.5) × 105 −3.8 ± 0.1 1.8 ± 0.1
HXLV-AC 25 (5.5 ± 0.6) × 105 −2.1 ± 0.1 1.9 ± 0.1
HXLV-AC 30 (4.2 ± 0.5) × 105 −2.8 ± 0.1 1.9 ± 0.1
HXLV-AC 35 (5.4 ± 0.5) × 105 −3.4 ± 0.1 1.8 ± 0.1
HXLV-AC 40 (1.1 ± 0.1) × 106 −4.0 ± 0.1 1.7 ± 0.1
a

Buffer conditions were as described in the footnote to Table 2. The listed values of K, ΔH, and N were derived from fits of ITC profiles (as shown in Fig. 7 for HXDV) with a model one set of binding sites. The indicated uncertainties reflect the standard deviations of the experimental data points from the fitted curves.