Biophysics Department, Faculty of Science, Cairo University, Giza, 12613, Egypt
Bovine serum albumin (BSA), in the solid state, was exposed to 50 Hz magnetic field of 10 gauss (1 mT) and 20 gauss (2 mT) for one hour. The changes in the secondary and tertiary structure of BSA were investigated. The Fourier transform infrared spectroscopy (FTIR) indicated that there is a relative decrease in absorption intensity of the amide I and amide II bands for the BSA exposed to 20 gauss 50 Hz magnetic field. The second derivative and multi-peak fitting of the amide I peak of the resultant spectrum indicated that there is a relative variation in the secondary structure of BSA exposed to 20 gauss magnetic field.
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