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Proceedings Paper

Luciferase intramolecular dynamics studied by time-resolved fluorescence spectroscopy
Author(s): Lubov Yu. Brovko; Andrey Yuri Chikishev; Olga A. Gandelman; Aleksandr P. Shkurinov
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Paper Abstract

Earlier a comprehensive study of reaction substrate, product and their complexes with the enzyme has been carried out by means of stationary fluorescence spectroscopy. A hypothesis has been suggested according to which protein changes its conformation during the reaction. In this respect it is quite interesting to study both static and dynamic properties of the enzyme molecule. Luckily, according to genetic engineering data, luciferase molecule contains only one tryptophan residue, which makes it a very convenient object for the studies by means of time-resolved fluorescence spectroscopy. The scope of this paper is the study of luciferase tryptophan fluorescence. The methods applied were fluorescence spectrochronography and anisotropy decay analysis.

Paper Details

Date Published: 17 June 1993
PDF: 5 pages
Proc. SPIE 1921, Laser Spectroscopy of Biomolecules, (17 June 1993); doi: 10.1117/12.146114
Show Author Affiliations
Lubov Yu. Brovko, Moscow State Univ. (Russia)
Andrey Yuri Chikishev, Moscow State Univ. (Russia)
Olga A. Gandelman, Moscow State Univ. (Russia)
Aleksandr P. Shkurinov, Moscow State Univ. (Russia)

Published in SPIE Proceedings Vol. 1921:
Laser Spectroscopy of Biomolecules
Jouko E. Korppi-Tommola, Editor(s)

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