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.