Abstract
Fourier transform infrared (FTIR) difference spectroscopy was used to study the effects of microwaves radiation on the structure of bacteriorhodopsin under light condition. The detailed FTIR spectral analysis revealed the pronounced structural changes in amide I and amide II regions as well as the rearrangements of the hydrogen-bonding network. Well-resolved peaks of amide bands allow accurate determination of two different components (α-I and α-II) of an α-helical conformation of opsin. Irreversible conformational changes of bacteriorhodopsin in purple membranes, detected by FTIR difference spectroscopy, suggest that regardless of temperature, microwaves induce protein structural rearrangements.
Published Version
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