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Proceedings Paper

Timeresolved Ftir Difference Spectroscopy Applied To Ultrathin Layers Of Membrane Proteins
Author(s): Klaus Gerwert; Georg Souvignier; Benno Hess
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Paper Abstract

ΔTo get insight in the function of proteins on an atomic level is a challenge of life science today. By x-ray-structure-analysis the architecture of a lot of proteins was obtained at atomic resolution. In order to understand the function of these structures, time resolved methods have to be developed. Using the Laue method, time resolved x-ray-structure-analysis seems to become applicable in the future. But this technique only gives a snapshot of an activated protein state during a reaction. In contrast, time resolved FTIR difference spectroscopy is able to monitor reaction kinetics of single amino acid side chains, e.g. protonation changes of internal aspartic acid residues, and of conformational changes of the protein backbone (1)(2)(3). By this technique interferograms are taken in a rapid scan mode before and after initiation of the investigated process. Difference spectra are computed between absorbance spectra of the ground state and the activated state. The scantime T is determined by the velocity of the scanner Vscan and the spectral resolution Δυ: T = 1/2 1/Δυ l/vscan. For 8 cm-1 spectral resolutionn a scantime T of 10 ms is yielded. The repetition rate between two scans is 44 ms.

Paper Details

Date Published: 1 December 1989
PDF: 2 pages
Proc. SPIE 1145, 7th Intl Conf on Fourier Transform Spectroscopy, (1 December 1989); doi: 10.1117/12.969390
Show Author Affiliations
Klaus Gerwert, Max-Planck-Institut fur Ernahrungsphysiologie (Germany)
Georg Souvignier, Max-Planck-Institut fur Ernahrungsphysiologie (Germany)
Benno Hess, Max-Planck-Institut fur Ernahrungsphysiologie (Germany)

Published in SPIE Proceedings Vol. 1145:
7th Intl Conf on Fourier Transform Spectroscopy
David G. Cameron, Editor(s)

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