Rheology of clustering protein solutions

Here we explore the rheology of low-salt lysozyme solutions, with special interest in the extremes of high concentration and low temperature. Under these conditions, reversible clustering of protein governed by their competing short-range attraction and long-range repulsion markedly enhances viscosity. Even in these conditions, the solutions exhibit Newtonian behavior over a wide range of shear rates. To test for departures from Newtonian behavior, we examined still higher shear rates. At shear rates in excess of 10,000 /s, we find reversible shear thinning at 40 {\%} mass fraction. These results reveal dynamics of the protein clusters and are compared with other measurements of solution dynamics by neutron spin echo scattering and dynamic light scattering.