17 June 1993 Luciferase intramolecular dynamics studied by time-resolved fluorescence spectroscopy
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Proceedings Volume 1921, Laser Spectroscopy of Biomolecules; (1993) https://doi.org/10.1117/12.146114
Event: Laser Spectroscopy of Biomolecules: 4th International Conference on Laser Applications in Life Sciences, 1992, Jyvaskyla, Finland
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.
© (1993) COPYRIGHT Society of Photo-Optical Instrumentation Engineers (SPIE). Downloading of the abstract is permitted for personal use only.
Lubov Yu. Brovko, Lubov Yu. Brovko, Andrey Yuri Chikishev, Andrey Yuri Chikishev, Olga A. Gandelman, Olga A. Gandelman, Aleksandr P. Shkurinov, Aleksandr P. Shkurinov, } "Luciferase intramolecular dynamics studied by time-resolved fluorescence spectroscopy", Proc. SPIE 1921, Laser Spectroscopy of Biomolecules, (17 June 1993); doi: 10.1117/12.146114; https://doi.org/10.1117/12.146114

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