Related Experiment Video
Updated: Jun 27, 2026
A Fluorescence Fluctuation Spectroscopy Assay of Protein-Protein Interactions at Cell-Cell Contacts
Published on: December 1, 2018
Fluorescence spectra study the perturbations of CopC native fold by 2-p-toluidinynaphthalene-6-sulfonate
Huiqing Li1, Yaqin Zhao, Xiaoyan Zhen
1Institute of Molecular Science, Key Laboratory of Chemical Biology and Molecular Engineering of Ministry of Education, Shanxi University, Taiyuan, Shanxi 030006, PR China.
Abstract:
2-p-Toluidinynaphthalene-6-sulfonate (TNS) was discovered to perturb native fold of CopC protein and to induce loss of biological activity to some extent which was dependent on TNS concentration. Hydrophobic and electrostatic interactions were revealed to account for the perturbation by comparison with some analogy. TNS, with far low concentration of 10(-5) to 10(-4)M, is presented as a denaturant. So TNS should be deliberated in detecting macromolecular conformation change as single evidence at higher concentration.
Related Concept Videos
01:29Atomic Fluorescence Spectroscopy
01:19Protein 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...