1 December 1989 Timeresolved FTIR Difference Spectroscopy Applied To Ultrathin Layers Of Membrane Proteins
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Proceedings Volume 1145, 7th Intl Conf on Fourier Transform Spectroscopy; (1989) https://doi.org/10.1117/12.969390
Event: Seventh International Conference on Fourier and Computerized Infrared Spectroscopy, 1989, Fairfax, VA, United States
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.
© (1989) COPYRIGHT Society of Photo-Optical Instrumentation Engineers (SPIE). Downloading of the abstract is permitted for personal use only.
Klaus Gerwert, Klaus Gerwert, Georg Souvignier, Georg Souvignier, Benno Hess, Benno Hess, } "Timeresolved FTIR Difference Spectroscopy Applied To Ultrathin Layers Of Membrane Proteins", Proc. SPIE 1145, 7th Intl Conf on Fourier Transform Spectroscopy, (1 December 1989); doi: 10.1117/12.969390; https://doi.org/10.1117/12.969390

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