Abstract
The opus of Don Winzor in the fields of physical and analytical biochemistry is a major component of that certain antipodean approach to this broad area of research that blossomed in the second half of the twentieth century. The need to formulate problems in terms of thermodynamic nonideality posed the challenge of describing a clear route from molecular interactions to the parameters that biochemists routinely measure. Mapping out this route required delving into the statistical mechanics of solutions of macromolecules, and at every turn mathematically complex, rigorous, general results that had previously been derived previously, often by Terrell Hill, came to the fore. Central to this work were the definition of the "thermodynamic activity", the pivotal position of the polynomial expansion of the osmotic pressure in terms of molar concentration and the relationship of virial coefficients to details of the forces between limited-size groups of interacting molecules. All of this was richly exploited in the task of taking account of excluded volume and electrostatic interactions, especially in the use of sedimentation equilibrium to determine values of constants for molecular association reactions. Such an approach has proved relevant to the study of molecular interactions generally, even those between the main macromolecular solute and components of the solvent, by using techniques such as exclusion and affinity chromatography as well as light scattering.