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Proceedings Paper

Biomedical applications of FTIR difference spectroscopy
Author(s): David Alan Moss; Kathrin Fuechsle; Ralf Masuch; Andreas Wolf
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Paper Abstract

FTIR spectroscopy of proteins has the unusual disadvantage of providing too much information. Thousands of individual bands contribute to the spectrum, leading to an overlap so extensive that essentially all detail is obscured. FTIR difference spectroscopy is a perturbation approach designed to overcome this problem: instead of the compete FTIR spectrum, only the changes in the spectrum in response to a biologically interesting perturbation of the same are recorded. The resulting difference spectra are far simpler than complete IR spectra, and thus can be interpret at the level of individual molecular bonds. But at the same time, they retain all the information pertaining to the structural dynamics related to the protein's catalytic cycle, and are thus of direct relevance to the study of molecular mechanisms in protein reactions. This paper presents our recent progress in the development of electrochemical, rapid mixing and flow techniques as triggers for FTIR difference spectroscopy, and the potential of such techniques as an analytical tool for biomedical research and in clinical diagnostics.

Paper Details

Date Published: 8 May 2000
PDF: 7 pages
Proc. SPIE 3918, Biomedical Spectroscopy: Vibrational Spectroscopy and Other Novel Techniques, (8 May 2000); doi: 10.1117/12.384962
Show Author Affiliations
David Alan Moss, Karlsruhe Research Ctr. (Germany)
Kathrin Fuechsle, Karlsruhe Research Ctr. (Germany)
Ralf Masuch, Karlsruhe Research Ctr. (Germany)
Andreas Wolf, Karlsruhe Research Ctr. (Germany)

Published in SPIE Proceedings Vol. 3918:
Biomedical Spectroscopy: Vibrational Spectroscopy and Other Novel Techniques
Anita Mahadevan-Jansen; Gerwin J. Puppels, Editor(s)

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