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ABSTRACT
Samples of hemoglobin and bovine serum albumin in different bi-distilled water solutions were exposed to a 50 Hz electromagnetic field at the intensity of 1 mT to investigate the response of hydrogen bonding to the applied field after exposure of 3 h by means of Fourier Transform Infrared spectroscopy. Spectral analysis evidenced a significant decrease in the absorbance signal of the Amide I vibration in exposed samples of hemoglobin and bovine serum albumin water solutions. In addition, Fourier self-deconvolution analysis and min-max normalization applied in the mid-infrared region to exposed and unexposed hemoglobin samples revealed a significant increase in the absorbance signal of the Amide II band and an up-shift toward the high energies of 1.5 cm−1 after exposure. Similar findings were observed after exposure of bovine serum albumin. These results can be easily explained assuming that hydrogen bonding in the secondary structure of these proteins in bi-distilled water solutions was enhanced after exposure to 50 Hz electromagnetic field.