Abstract
FT-IR difference spectra for the photoreactions of bacteriorhodopsin (bR) are compared to difference spectra of polyamide-6 and -11 obtained during uniaxial elongation. The purple membrane was hydrated with D2O in order to identify bands above 3000 cm−1. In the bR photocycle (bR → K), the difference spectra in D2O closely match the band contour found in the difference spectra of elongated polyamide-11. The data suggest that a structural change occurs in the backbone of the membrane protein bacteriorhodopsin, resulting in weakened and strengthened hydrogen bonds of the amide functionality of the backbone.
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