Session C1 - Poster Session I.
POSTER session, Monday afternoon, March 03
Room Exhibit Hall 2/3, Austin Convention Center
Fluorescent Proteins (FPs) have become extremely popular in life science research as protein labels, markers of gene expression and reporters of environmental conditions in living cells. The fluorescent protein eqFP611, cloned from the sea anemone Entacmaea quadricolor, has the largest Stokes shift (52 nm) and the most red-shifted fluorescence emission (611 nm) of all non-modified FPs that are currently available in recombinant form. Other properties make it even more advantageous for biological applications: pH independent fluorescence emission in the pH range 4 – 11, fast and complete maturation of the fluorophore and reduced oligomerization tendency. To examine the photophysical properties of eqFP611, we have measured absorption, excitation, and emission spectra using bulk spectroscopy in a wide temperature range (12 – 350 K). From these data, the temperature dependencies of the quantum yield, electron-vibronic coupling factors, and oscillator strength of the electronic transition have been determined. Moreover, we have studied the fluorescence emission using fluorescence correlation spectroscopy (FCS) and single-molecule studies. We present a quantitative model of the light-driven dynamics.