Photophysics and dihedral freedom of the chromophore in yellow, blue, and green fluorescent protein.

ABSTRACT: Green fluorescent protein (GFP) and GFP-like fluorescent proteins owe their photophysical properties to an autocatalytically formed intrinsic chromophore. According to quantum mechanical calculations, the excited state of chromophore model systems has significant dihedral freedom, which may lead to fluorescence quenching intersystem crossing. Molecular dynamics simulations with freely rotating chromophoric dihedrals were performed on green, yellow, and blue fluorescent proteins in order to model the dihedral freedom available to the chromophore in the excited state. Most current theories suggest that a restriction in the rotational freedom of the fluorescent protein chromophore will lead to an increase in fluorescence brightness and/or quantum yield. According to our calculations, the dihe

SUBMITTER: Megley CM 

PROVIDER: S-EPMC2671006 | biostudies-literature | 2009 Jan

REPOSITORIES: biostudies-literature