Cold gelation behavior of BSA protein has been studied mixing with mono-, di- and tri-valent ions at pD ≈ 7.0. Small angle neutron scattering (SANS) studies show that for the heat treated BSA fractal structure grows with the addition of salts. Heat treated BSA without salt shows intermediate range electrostatic repulsion and long range attraction. However, in presence of salts, cold gelation occurs but the fractal dimension depends upon the salt type and salt concentration. Variation of fractal dimension with salt concentration is nearly similar for Cu²⁺ and Fe³⁺ ions however similarity exists between Na⁺ and Ca²⁺ ions.