Determination of the binding constant of ligand to protein by thermal inactivation tehnique. Effect of two binding sites.
Theoretical considerations on the determining the binding constants (eta) of ligands to proteins were carried out. Whereas for a one-subunit protein the relationship between thermal inactivation rates and ligand concentration there is a simple linear function, for a protein with two subunits, a second-order relationship is derived. If the theory for one-subunit proteins is applied to multi-subunit proteins, the derived values of eta tend to be lower than the real binding constants. A method of determining the ligand binding constant for a two-subunit protein is described.
D001665:Binding Sites; D007700:Kinetics; D008024:Ligands; D008433:Mathematics; D008722:Methods; D011485:Protein Binding; D011506:Proteins
D008024:Ligands; D011506:Proteins