Protein–protein interactions in solutions are easily detected by the commonly used methods of molecular transport, such as electrophoresis, sedimentation, and chromatography. In contrast, it is very difficult to determine unambiguously the stoichiometry and thermodynamic parameters of any such interactions. This chapter describes preliminary steps that can be helpful to proceed from the initial recognition of the presence of interactions toward an understanding of their nature and magnitude. For this purpose, the chapter presents the way to simulate boundary patterns for reversibly reacting systems, which can be used for comparison with actual transport experiments. Chemical equilibria involving macromolecules are usually examined by equilibrium techniques, such as light scattering, equilibrium sedimentation, and osmotic pressure. These measurements define the dependence of various molecular weight averages on solute concentration. The treatment of macromolecular interactions by equilibrium methods makes heavy demands on the quality of the data and is sensitive to vexing artifacts, particularly if macromolecular contaminants are present that do not participate in chemical equilibrium. © 1978, Elsevier Inc. All rights reserved.
Gilbert, L. M., & Gilbert, G. A. (1978). Molecular Transport of Reversibly Reacting Systems: Asymptotic Boundary Profiles in Sedimentation, Electrophoresis, and Chromatography. Methods in Enzymology, 48(C), 195–212. https://doi.org/10.1016/S0076-6879(78)48011-5