Abstract
Protein-nucleic acid and protein-protein interactions have been studied by a variety of biochemical and physicochemical techniques, each of which has distinctive advantages and disadvantages. In particular, analytical ultracentrifugation has the advantages that it is rigorously based upon reversible thermodynamics, and the reactants and product or products of an interaction each have uniquely defined concentration gradients that can be resolved by appropriate mathematical analysis to give the desired values of the natural logarithms of the equilibrium constants with a minimum of assumptions.
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