Novel fluorophores based on the green fluorescent protein

ORGN 42

Laren M. Tolbert, laren.tolbert@chemistry.gatech.edu, Kyril M Solntsev, solntsev@gatech.edu, Jian Dong, gtg907p@mail.gatech.edu, and Anthony Baldridge, abaldridge3@mail.gatech.edu. School of Chemistry and Biochemistry, Georgia Institute of Technology, Atlanta, GA 30332-0400
Removal of the green fluorescent protein chromophore from its protective protein ß-barrel causes a dramatic drop in fluorescence quantum yield, presumably because of facile twisting about the formal double bond in the excited state. We have been exploring methods for using inhibition of twisting as a way of developing sensitive fluorophores for molecular environments, using substituents on the fluorophores to inhibit bond rotation as a function of environment. Recent progress in this area will be discussed.

 

Novel Fluorophores
1:00 PM-5:30 PM, Sunday, April 6, 2008 Morial Convention Center -- Rm. R05, Oral

Division of Organic Chemistry

The 235th ACS National Meeting, New Orleans, LA, April 6-10, 2008