This study explores the impact of salt concentration and the degree of hydration on the structure of bovine serum albumin (BSA) using vibrational spectroscopy methods, specifically Fourier transform infrared spectroscopy and  Raman scattering. BSA, a key plasma protein, plays essential roles in binding and transporting various molecules in the bloodstream. The research focuses on understanding how do the interaction with ions and water molecules  affect the secondary and tertiary structure of globular proteins, emphasizing the significance of environmental factors in protein conformation. The results indicate distinct responses in the vibrational spectra of BSA to the presence  of salt. Analysing the Amide I band give the parameters of the secondary structure of BSA. In all systems investigated the values obtained is in good correspondence with the data for native BSA, but the secondary and tertiary BSA  structure in dehydrated films containing NaCl is closer to native, hence ions prevent albumin from denaturation and β-aggregation.