Thermodynamics and kinetics of co-operative protein-nucleic acid binding. I. General aspects of analysis of data.
The process under consideration is the binding of a ligand to a linear polymer of equivalent subunits such that each bound molecule of ligand occupies n subunits. Interactions between bound ligand molecules are also considered. Some useful points regarding the evaluation of raw data without recourse to any specific binding mechanism are discussed first. For a treatment in terms of appropriate thermodynamic parameters a simple model is examined in greater detail. It assumes that interactions are limited to those between ligands bound to nearest-neighbour positions on the polymer. Exact expressions for some basic binding properties of this model at equilibrium are developed. The relations can be considerably simplified in the case of pronounced positive co-operativity which is frequently encountered in practice. Appropriate plots of the data to test the model and to evaluate its parameters are proposed. A simple but consistent kinetic scheme is also introduced. It allows calculation of relaxation times as they can be measured by means of special techniques.
D001704:Biopolymers; D004247:DNA / Q000378:metabolism*; D007700:Kinetics; D008024:Ligands; D008433:Mathematics; D008956:Models, Chemical; D011485:Protein Binding; D011506:Proteins / Q000378:metabolism*; D013816:Thermodynamics
D001704:Biopolymers; D008024:Ligands; D011506:Proteins; D004247:DNA