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D. I. de Pomerai, B. Smith, A. Dawe, K. North, T. Smith, D. B. Archer, I. R. Duce, D. Jones and P.M. Candido, “Microwave Radiation can Alter Protein Conformation without Bulk Heating,” FEBS Letters, Vol. 543, No. 1-3, 2003, pp. 93-97.

has been cited by the following article:

• TITLE: Inspections of Mobile Phone Microwaves Effects on Proteins Secondary Structure by Means of Fourier Transform Infrared Spectroscopy

  AUTHORS: Emanuele Calabrò, Salvatore Magazù

  KEYWORDS: Mobile Phone, Microwaves, Protein, Infrared Spectrum, Secondary Structure, Amide I

  JOURNAL NAME: Journal of Electromagnetic Analysis and Applications, Vol.2 No.11, December 1, 2010

  ABSTRACT: In this study the effects of microwaves on the secondary structure of three typical proteins have been investigated. A set of samples of lysozyme, bovine serum albumin and myoglobin in D2O solutions were exposed for 8 hours to mobile phone microwaves at 900 MHz at a magnetic field intensity around 16 mA/m. The relative effects on the secondary structure of the proteins were studied by means of Fourier Transform Infrared Spectroscopy. An increase of the amide I band intensity in the secondary structure of the proteins was observed after the microwaves exposure. Furthermore, a weak shift of the amide I mode of bovine serum albumin and a heavier shift of the amide I of myoglobin occurred after the exposure. In addition, a clear increasing of the β-sheet components with respect to the α-helix content was observed in the spectra of bovine serum albumin and myoglobin after the exposure, suggesting the hypothesis of the formation of aggregates.