Ligand binding and self-association of proteins.
This review deals with the quantitative analysis of protein self-association and ligand binding when there is a signficant mutual influence of the two processes. The particular points of interest are the evaluation of the pertinent equilibrium constants and the prediction and interpretation of concentration profiles in transport experiments, including gel elution and sedimentation velocity. The case of dimertetramer equilibrium with four binding sites for ligand is considered in detail. Three representative experimental studies are described which deal with hemoglobin, phosphorylase b, and tubulin.
D000818:Animals; D002417:Cattle; D002850:Chromatography, Gel; D006441:Hemoglobin A; D006801:Humans; D007700:Kinetics; D008024:Ligands; D008433:Mathematics; D008956:Models, Chemical; D010108:Oxyhemoglobins; D006005:Phosphorylases; D011487:Protein Conformation; D011506:Proteins; D014404:Tubulin
D008024:Ligands; D010108:Oxyhemoglobins; D011506:Proteins; D014404:Tubulin; D006441:Hemoglobin A; D006005:Phosphorylases