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Proceedings Paper

Structure-Activity Relations In Enzymes: An Application Of IR-ATR Modulation Spectroscopy
Author(s): Urs P. Fringeli; Peter Ahlstrom; Claudius Vincenz; Marianna Fringeli
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Paper Abstract

Relations between structure and specific activity in immobilized acetylcholinesterase (ACNE) have been studied by means of pH- and Ca++-modulation technique combined with attenuated total reflection (ATR) infrared (IR) spectroscopy and enzyme activity measurement. Periodic modulation of pH and Ca++-concentration enabled a periodic on-off switching of about 40% of the total enzyme activity. It was found that about 0.5 to 1% of the amino acids were involved in this process. These 15 to 30 amino acids assumed antiparallel pleated sheet structure in the inhibited state and random and/or helical structure in the activated state.

Paper Details

Date Published: 20 December 1985
PDF: 2 pages
Proc. SPIE 0553, Fourier and Computerized Infrared Spectroscopy, (20 December 1985); doi: 10.1117/12.970787
Show Author Affiliations
Urs P. Fringeli, University of Vienna (Austria)
Peter Ahlstrom, Swiss Federal Institute of Technology (Switzerland)
Claudius Vincenz, Swiss Federal Institute of Technology (Switzerland)
Marianna Fringeli, Swiss Federal Institute of Technology (Switzerland)


Published in SPIE Proceedings Vol. 0553:
Fourier and Computerized Infrared Spectroscopy
David G. Cameron; Jeannette G. Grasselli, Editor(s)

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