Related Experiment Video
Updated: Aug 12, 2026

Examining the Conformational Dynamics of Membrane Proteins in situ with Site-directed Fluorescence Labeling
Published on: May 29, 2011
[Study of the cholinesterase active site using a fluorescent probe]
D O Vetkin1, E T Gaĭnullina, V A Karavaev
1Faculty of Physics, Moscow State University, Vorob'evy gory, Moscow, 119992 Russia.
Abstract:
We studied fluorescence of 9-amino-1,2,3,4-tetrahydroacridine hydrochloride (tacrine) in the presence of serum cholinesterase. Quenching of tacrine fluorescence dependent on cholinesterase activity has been revealed. A quenching mechanism is proposed; it includes formation of a complex and charge transfer mediated by excited tacrine molecule as well as indole of tryptophan residue from the periphery of cholinesterase active site.
Related Concept Videos
Labeling DNA Probes
Radioisotopes, fluorophores, or small molecule binding partners like biotin or digoxigenin, are the most widely used reporter tags for labeling DNA probes. These labels can be attached to the probe DNA molecule via...
Protein Dynamics in Living Cells
Fluorescent recovery after photobleaching (FRAP) is a fluorescent-protein-based detection technique used to quantify protein movement rates within the cell. This method exposes a small portion of the cell to an intense laser beam. The laser beam causes permanent photobleaching of the fluorophore-tagged proteins in the exposed region. As the bleached...

