The influence of radio-frequency radiation on thermal stability of bovine serum albumin in aqueous solution

Protein unfolding events were studied by differential scanning calorimetry (DSC) for bovine serum albumin (BSA) aqueous solutions exposed to radio-frequency radiation. No immediate effect of this radiation on thermal unfolding of BSA was observed. The differences between irradiated and control samples have appeared during the storage of BSA solution. The irradiated samples changed faster than non-irradiated. Our results indicated that the age-related changes were stronger for 3.5 and 5 MHz than for 247 MHz frequency and dependent on energy power of radiation. Deconvolution of DSC traces allowed to study the effect of radio-frequency radiation on each component transition. This revised version was published online in July 2006 with corrections to the Cover Date.