In experiment the luminescence of the green fluorescent (GFP) molecule has been known to be suppressed by compression using the atomic force microscope (AFM) ti
p. One of the possible mechanisms has been studied in our previous work using the all-atom force field calculation combined with the quantum mechanical electronic states calculation. We have shown that at 0 K the mechanical force by the tip breaks down the hydrogen bonding network around the chromophore, which brings about the quenching of radiation process[1]. Recently, as a second step, we newly started to study the structural change of a GFP molecule in a realistic situation, i.e., in solvent at 310 K. In the poster, we will show the detailed features of the force curve and structural change of the molecule.
[1] "Quenching Mechanism of Mechanically Compressed Green Fluorescent Protein Studied by CASSCF/AM1",
Q. Gao, K. Tagami, M. Fujihira and M. Tsukada,
Jpn. J. Appl. Phys. 45 (2006) L929-L931. |