Structure-Activity Relations In Enzymes: An Application Of IR-ATR Modulation Spectroscopy

Urs P. Fringeli; Peter Ahlstrom; Claudius Vincenz; Marianna Fringeli

doi:10.1117/12.970787

20 December 1985 Structure-Activity Relations In Enzymes: An Application Of IR-ATR Modulation Spectroscopy

Urs P. Fringeli, Peter Ahlstrom, Claudius Vincenz, Marianna Fringeli

Proceedings Volume 0553, Fourier and Computerized Infrared Spectroscopy; (1985) https://doi.org/10.1117/12.970787
Event: 1985 International Conference on Fourier and Computerized Infrared Spectroscopy, 1985, Ottawa, Canada

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.

Citation Download Citation

Urs P. Fringeli, Peter Ahlstrom, Claudius Vincenz, and Marianna Fringeli "Structure-Activity Relations In Enzymes: An Application Of IR-ATR Modulation Spectroscopy", Proc. SPIE 0553, Fourier and Computerized Infrared Spectroscopy, (20 December 1985); https://doi.org/10.1117/12.970787

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