Related Experiment Video
Updated: Jul 23, 2026

Fluorescence Anisotropy as a Tool to Study Protein-protein Interactions
Published on: October 21, 2016
Interaction of aromatic compounds with Photobacterium leiognathi luciferase: fluorescence anisotropy study
N S Kudryasheva1, E V Nemtseva, A J W G Visser
1Institute of Biophysics, SB RAS, 660036 Krasnoyarsk, Russia. qdr@akadem.ru
Abstract:
The time-resolved and steady-state fluorescence techniques were employed to elucidate possible interactions of four aromatic compounds (anthracene, POPOP, MSB and 1,4-naphthalendiol) with bacterial luciferase. Fluorescence spectra and fluorescence anisotropy decays of these compounds were studied in ethanol, water-ethanol solutions and in the presence of bacterial luciferase. Shifts of fluorescent spectra and differences in rotational correlation times are interpreted in terms of weak (hydrophobic) interactions of the molecules with the enzyme. These interactions suggest the feasibility of intermolecular energy transfer by an exchange resonance mechanism with a collision-interaction radius as a way of excitation of these compounds in the reaction catalysed by bacterial luciferase.
More Related Videos
07:55Luciferase Complementation Imaging Assay in Nicotiana benthamiana Leaves for Transiently Determining Protein-protein Interaction Dynamics
Published on: November 20, 2017
05:52In Situ Measurement and Correlation of Cell Density and Light Emission of Bioluminescent Bacteria
Published on: June 28, 2018
Related Concept Videos
Photochemical Electrocyclic Reactions: Stereochemistry
Selection Rules: Photochemical Activation
Variables Affecting Phosphorescence and Fluorescence
Photoluminescence: Applications