Investigation on the Binding and Conformational Change of All-trans-Retinoic Acid with Peptidyl Prolyl cis/trans Isomerase Pin1 Using Spectroscopic and Computational Techniques

Table 1

Thermodynamic parameters of the Pin1-ATRA complex at different temperatures.

Parameters	293 K	303 K
Ksv (10^5 mol/L)	1.83 ± 0.01	1.32 ± 0.01
R^2a	0.993	0.996
n	0.73 ± 0.02	0.73 ± 0.03
Ka (10^5 mol/L)	2.90 ± 0.02	2.06 ± 0.01
R^2b	0.998	0.996
ΔG (kJ/mol)	−30.64 ± 0.09	−29.80 ± 0.34
ΔH (kJ/mol)	15.76 ± 0.88	15.76 ± 0.88
ΔS (J/mol/K)	158.36 ± 0.34	154.91 ± 0.42