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Updated: Jul 6, 2026

Determination of Protein-ligand Interactions Using Differential Scanning Fluorimetry
Published on: September 13, 2014
How deep is the potential well confining a protein in a specific conformation? A single-molecule study on temperature
Hiroyuki Oikawa1, Satoru Fujiyoshi, Takehisa Dewa
1Department of Physics, Tokyo Institute of Technology, Meguro 152-8551, Japan.
Abstract:
The fluorescence excitation spectrum of a single chromophore molecule in a photosynthetic pigment-protein complex is known to change in time at liquid helium temperature. The spectral change reflects a conformational change of the protein to which the chromophore binds. This work follows the temporal behavior of the spectrum of a single chromophore in the temperature range between 5 adn 18 K. The temperature dependence reveals two types of conformational change of the protein, i.e., thermally activated motions over a potential barrier of ca. 0.1 kJ/mol and temperature-independent motions of tunneling of a proton.
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