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Comparison of Bacteriorhodopsin Conformational Changes with Uniaxially Elongated Aliphatic Polyamide Samples by Using FT-IR Difference Spectroscopy

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Progress in Fourier Transform Spectroscopy

Part of the book series: Mikrochimica Acta Supplement ((MIKROCHIMICA,volume 14))

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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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© 1997 Springer-Verlag Wien

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Fischer, W.B., Wu, P., Hoffmann, U., Eichhorn, KJ., Siesler, H.W., Rothschild, K. (1997). Comparison of Bacteriorhodopsin Conformational Changes with Uniaxially Elongated Aliphatic Polyamide Samples by Using FT-IR Difference Spectroscopy. In: Mink, J., Keresztury, G., Kellner, R. (eds) Progress in Fourier Transform Spectroscopy. Mikrochimica Acta Supplement, vol 14. Springer, Vienna. https://doi.org/10.1007/978-3-7091-6840-0_103

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  • DOI: https://doi.org/10.1007/978-3-7091-6840-0_103

  • Publisher Name: Springer, Vienna

  • Print ISBN: 978-3-211-82931-8

  • Online ISBN: 978-3-7091-6840-0

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