Table 2.

Thermodynamic parameters for DRV binding determined by ITC

Protein	KA (M−1)	KL (nM)a	ΔH (kcal/mol)	−TΔS (kcal/mol)	ΔG (kcal/mol)
PRb	2.2 × 1011	0.005	−12.1	−3.1	−15.2
PR20c	2.45 ± 0.59 × 107	41 ± 10	−7.6 ± 0.1	−2.6	−10.2
PRD25Nd	3.17 ± 0.29 × 105	3,200 ± 293	−5.8 ± 0.2	−1.8	−7.6
ANAM-11c	6.2 ± 3.4 × 108	1.6 ± 0.8	−10.0 ± 0.07	−2.1	−12.1

All titrations, unless noted otherwise, were performed in 50 mM sodium acetate buffer at pH 5.0 and 28 °C as described.⁹ The thermodynamic parameters for PR20 and ANAM-11 are reported here for the first time. Other values incorporated in the table are solely for comparison.

^aDissociation constant equal to 1/K_A

^bFor wild-type PR, in 10 mM sodium acetate buffer, pH 5, at 20 °C³⁸

^creference⁹

^dreference²¹