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In this work the study of the effect of millimeter range electromagnetic waves (MM EMW) on the complexes of human serum albumin (HSA) with methyl violet (MV) has been carried out at the different frequencies, using the methods of fluorescence and thermodenaturation. It was shown that MV binds to HSA, forming a complex, and increasing of the intensity of the protein own fluorescence takes place, meanwhile the stabilization of HSA increases. MM EMW irradiation of HSA by various frequencies invokes additional changes in the protein structure. Thus, at the protein irradiation with the frequency 41.8 GHz the protein stabilization increases as well as hydrophobicity around the tryptophan rises, while at the irradiation with 51.8 GHz the stabilization is expressed less and the hydrophobicity enhancement around the tryptophan can be neglected. [ABSTRACT FROM AUTHOR]

The effect of electromagnetic waves of the millimeter region on the conformation and fluorescence characteristics of human serum albumin was studied. It is shown that the irradiation of the albumin solution leads to an increase of the fluorescence intensity depending on the duration of irradiation. At an irradiation frequency of 48 GHz the fluorescence intensity of albumin hardly changes at all, while at 41.8 and 51.8 GHz it increases. It is also shown that when the irradiation frequency is 51.8 GHz, the intensity of the albumin solution fluorescence increases with increase of the irradiation time. [ABSTRACT FROM AUTHOR]