A Diversified Spectrometric and Molecular Docking Technique to Biophysical Study of Interaction between Bovine Serum Albumin and Sodium Salt of Risedronic Acid, a Bisphosphonate for Skeletal Disorders

Table 2

Binding constants, number of binding sites, and thermodynamic parameters for the interaction of BSA with RSN at different temperatures (pH 7.40).

Compound	Temperature (K)	()  10^5		()	()	()
BSA-RSN	289	3.51 ± 0.10	1.196	−30.62	−38.83	−28.408
	297	1.95 ± 0.04	1.110	−30.39
	305	1.45 ± 0.07	1.067	−30.16

is the binding constant; is the number of binding sites; is the change in Gibb’s free energy; is change in enthalpy; is change in entropy.