A circular dichroism study of human erythrocyte ghost proteins during exposure to 2450 MHz microwave radiation.
The effect of 2450 MHz microwave radiation on the proteins of human erythrocyte ghosts has been investigated using circular dichroism spectroscopy. A specially constructed waveguide inserted into the spectropolarimeter allowed the continuous recording of optical activity before, during and after microwave irradiation. The data indicate that high levels of microwave radiation (600 mW/g, specific absorption rate) induce decreases in alpha-helical conformation that may result from both thermal vibrations and increased strain on the intramolecular hydrogen bonds that maintain secondary structure. The latter effect may result from differential intramolecular interactions with the oscillating electric field. Spectrin (bands 1 and 2) isolated from the ghosts was more sensitive to microwave irradiation than intact ghosts, and spectrin-depleted vesicles were the least sensitive. The data, therefore, indicate that the alpha-helical conformation of spectrin is altered by high levels of microwave radiation.
D002942:Circular Dichroism; D004910:Erythrocyte Membrane / Q000528:radiation effects*; D004912:Erythrocytes / Q000528:radiation effects*; D006358:Hot Temperature; D006801:Humans; D008565:Membrane Proteins / Q000528:radiation effects; D008872:Microwaves; D011487:Protein Conformation / Q000528:radiation effects; D013049:Spectrin / Q000528:radiation effects
D008565:Membrane Proteins; D013049:Spectrin