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We report on a joint experimental-theoretical study of collective diffusionin, and static shear viscosity of solutions of bovine serum albumin (BSA)proteins, focusing on the dependence on protein and salt concentration. Dataobtained from dynamic light scattering and rheometric measurements are comparedto theoretical calculations based on an analytically treatable spheroid modelof BSA with isotropic screened Coulomb plus hard-sphere interactions. The onlyinput to the dynamics calculations is the static structure factor obtained froma consistent theoretical fit to a concentration series of small-angle X-rayscattering (SAXS) data. This fit is based on an integral equation scheme thatcombines high accuracy with low computational cost. All experimentally probeddynamic and static properties are reproduced theoretically with an at leastsemi-quantitative accuracy. For lower protein concentration and low salinity,both theory and experiment show a maximum in the reduced viscosity, caused bythe electrostatic repulsion of proteins. The validity range of a generalizedStokes-Einstein (GSE) relation connecting viscosity, collective diffusioncoefficient, and osmotic compressibility, proposed by Kholodenko and Douglas[PRE 51, 1081 (1995)] is examined. Significant violation of the GSE relation isfound, both in experimental data and in theoretical models, in semi-dilutesystems at physiological salinity, and under low-salt conditions for arbitraryprotein concentrations.

Viscosity and Diffusion: Crowding and Salt Effects in Protein Solutions