Bioinorganic Chemistry and Applications / 2018 / Article / Tab 2

Research Article

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).

CompoundTemperature (K) ()  105 () () ()

BSA-RSN2893.51 ± 0.101.196−30.62−38.83−28.408
2971.95 ± 0.041.110−30.39
3051.45 ± 0.071.067−30.16

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.