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Updated: Jul 16, 2026

Using Three-color Single-molecule FRET to Study the Correlation of Protein Interactions
Published on: January 30, 2018
[Study on interaction between hypocrellin A and hemoglobin or myoglobin using synchronous fluorescence spectra]
Xiao-hong Wu1, Jia-hong Zhou, Xiao-tian Gu
1Analysis and Testing Center, Nanjing Normal University, Jiangsu Engineering Research Center of Bio-Medical Function Materials, Nanjing 210097, China.
The effects of hypocrellin A (HA) on the conformational changes of hemoglobin and myoglobin were studied using synchronous fluorescence spectroscopy. The results indicated that HA can change the conformation of these two proteins, leading to the change in the micro-environment of tryptophane and tyrosine residues from hydrophobic environment to hydrophilic environment to different extent.
The effects of hypocrellin A (HA) on the conformational changes of hemoglobin and myoglobin were studied using synchronous fluorescence spectroscopy. The results indicated that HA can change the conformation of these two proteins, leading to the change in the micro-environment of tryptophane and tyrosine residues from hydrophobic environment to hydrophilic environment to different extent.

