Analyzing the Size of Albumin Macromolecules in Aqueous Solutions

Changes in the structure and size of macromolecules of human and bovine serum albumin in aqueous solutions are considered, depending on temperature, concentration, and acid-base equilibrium. It is found that a change in the hydrodynamic radius of the macromolecule is an indicator of the structural phase transformations of globular proteins. Ways of determining the radii of macromolecules from data on the shear viscosity of solutions and the self-diffusion of macromolecules in them are discussed. The hydrodynamic radii of albumin macromolecules found by these means are compared. It is shown that conclusions can be drawn about the nature of bonding between water molecules and protein macromolecules using the obtained data.