The rheology of a temperature-induced protein bovine serum albumin gel is shown to strongly depend on the solution pH and protein concentration. Small-angle neutron scattering studies showed the presence of a fractal structure of the gels, resembling the aggregation of protein molecules and causing a three-dimensional network kind of arrangement. The fractal dimensions were observed to be constant and independent of the variation of pH and the protein concentration. The results of rheology and scattering experiments are correlated in terms of pH-dependent flexibility of flocs in the gels and hindrance to flow with concentration, while the structure of such flocs remains similar irrespective of the solution conditions.