a thermal accelerant are rare nonetheless calculated dipole moment of serum albumin in vacuum is very large 710 d d debye in comparison to the ta substance first described above cscl ca 10 d or compared to water 1 85 d despite its large dipole moment physiologically available bovine serum albumin bsa alone does not increase the temperature rapidly due to its low dielectric constant and the loss factor in the range of frequencies of interest i e 915 mhz 2 45 ghz 12 with 500 mg ml bsa a gradual increase to 40 50 u00b0 c was observed in vitro at 10 min for 60 w with a 915 mhz when the antenna was positioned a distance of 1 5 cm from the bsa sample the temperature increase was insufficient to make bsa alone as a ta furthermore the albumins of high concentrations gt 300 mg ml tend to have a very high viscosity due in most part to protein protein interactions as shown in fig9 which schematically illustrates the viscosity of bsa as a function of concentration under the applied microwave radiation the surface charges of the albumin molecule are occupied by the intermolecular interactions with the readily available other albumin molecules in order to relieve the interactions we used nacl as a chaotrope in essence it is believed that the intermolecular interactions of bsa molecules consist of charge charge dipole dipole as well as hydrophobic interactions and thus exhibit high viscosity by adding nacl to the solution the viscosity will be lowered by the salt ions competing with other bsa charges and subsequent solvation by water molecules this will free up the individual bsa molecules to respond to the microwave energy we have examined the effect of nacl on thermal acceleration efficiency of the albumin.