title: Determination of the binding constant of ligand to protein by thermal inactivation tehnique. Effect of two binding sites.
abstract: 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.
mesh_terms: D001665:Binding Sites; D007700:Kinetics; D008024:Ligands; D008433:Mathematics; D008722:Methods; D011485:Protein Binding; D011506:Proteins
chemical_list: D008024:Ligands; D011506:Proteins