Thermodynamic parameters of binding determined by isothermal titration calorimetry (ITC) for dsRNA-binding domains of MARV VP35 with different dsRNA molecules.

All reported values represent a calculated average determined from at least two independent measurements. Unless otherwise noted, the estimated error from replicate measurements is approximately 10% of the reported average values. Slight errors on the absolute stoichiometry values are also associated with errors in protein concentration measurements, as well as sample impurity. Superscripts A and B refer to events A and B wherever applicable. N represents number of molecules binding in that event (stoichiometry of binding).*The change in Gibbs free energy (ΔG) was determined using the equation: ΔGbinding = RTlnKd[47].&There are too few measured points to confidently determine the ΔGbinding or the Kd of the first binding event (stoichiometry below 0.2).$The standard deviation for this binding event derived from four independent measurements (NB±0.3 and KdB±16.5) is significantly higher than the estimated error associated with other measurements.