Abstract
A general monomer-dimer equilibrium system involving ligand interactions ispresented. Cooperativity features of specific limited models are analyzed by selecting the appropriate family of equilibrium constants from this general scheme. Each system is then characterized in terms of Hill coefficient dependency on alterations in values of equilibrium constants and total acceptor concentration. This method permits comparison of predicted cooperativity trends between systems. Contrasting reports concerning cooperativity dependencies for certain defined equilibrium systems are compared and the discrepancies resolved. Characteristics of cooperativity binding patterns are shown to include symmetry about dimerization association constant values, both positive and negative cooperativity for a single set of parameters, and significant changes in cooperativity features with relatively small changes in equilibrium parameters.
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Wolfer, G.K., Neil, J.L. & Rippon, W.B. Cooperativity of ligand binding as a function of monomer-dimer equilibrium parameters and acceptor concentration. J Protein Chem 6, 441–454 (1987). https://doi.org/10.1007/BF02343341
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DOI: https://doi.org/10.1007/BF02343341