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The effects of extremely low frequency electromagnetic field on the secondary structure of hemoglobin were investigated by means of Fourier Transform Infrared Spectroscopy. A decrease in intensity of the a-helix component in the amide I and amide II regions was observed after exposure of 4 h to a 50 Hz electromagnetic field at 1 mT. In addition, Fourier self deconvolution analysis was carried out on exposed and not-exposed spectra. A relative increase of the b-sheet feature in the amide I region was evidenced, showing that an unfolding process of the protein occurred after exposure to extremely low frequency electromagnetic field, suggesting the hypothesis of the formation of aggregates.

Unfolding-induced in Haemoglobin by Exposure to Electromagnetic Fields: A FTIR Spectroscopy Study