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On Mechanism of Enhanced Fluorescence in Green Fluorescent Protein

E Starikov ; Itai Panas (Institutionen för kemi- och bioteknik, Oorganisk miljökemi) ; Y MOCHIZUKI ; S TANAKA ; Y Luo ; H Ågren
Biophysical Reviews and Letters (1793-7035). Vol. 2 (2007), 3/4, p. 221-227.
[Artikel, refereegranskad vetenskaplig]

In spite of the numerous experimental and theoretical studies on green fluorescent protein and its modifications, there is still no definitive answer to the central question: why such systems exhibit enhanced fluorescence. Based upon detailed quantum-chemical estimations, we advocate the following hypothesis. In the green fluorescent protein ground electronic state, the protein surrounding strains the chromophore with respect to its native intramolecular conformational preference in vacuo or in solution. Absorbing a photon of the proper wavelength not only causes a joint proton–electron transfer in and around the chromophore, but also increases the intrinsic strain of the latter. Since conformational relaxation of such a structure will not require any additional energy input, the energy gained by the chromophore cannot be dissipated into the chromophore's internal non-radiative degrees of freedom, and thus it returns as a fluorescence emission.

Nyckelord: Green fluorescent protein, ab initio, semiempirical quantum chemistry

Denna post skapades 2008-06-26. Senast ändrad 2013-05-06.
CPL Pubid: 72181


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Institutioner (Chalmers)

Institutionen för kemi- och bioteknik, Oorganisk miljökemi (2005-2014)


Molekylär biofysik

Chalmers infrastruktur