20 December 1985 Structure-Activity Relations In Enzymes: An Application Of IR-ATR Modulation Spectroscopy
Author Affiliations +
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.
© (1985) COPYRIGHT Society of Photo-Optical Instrumentation Engineers (SPIE). Downloading of the abstract is permitted for personal use only.
Urs P. Fringeli, Urs P. Fringeli, Peter Ahlstrom, Peter Ahlstrom, Claudius Vincenz, Claudius Vincenz, Marianna Fringeli, 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); doi: 10.1117/12.970787; https://doi.org/10.1117/12.970787
PROCEEDINGS
2 PAGES


SHARE
Back to Top