Excited-state structure determination of the green fluorescent protein chromophore.
Ultrafast polarization-sensitive infrared (IR) spectroscopy of the C=O stretching mode of the chromophore of the green fluorescent protein reveals a near complete twisting around the ethylenic bridge between the phenolate and imidazolidinone groups upon electronic excitation, hinting at a decisive role of this motion in the efficient internal conversion process.
Usman
Anwar
A
Max Born Institut für Nichtlineare Optik und Kurzzeitspektroskopie, Max Born Strasse 2A, D-12489 Berlin, Germany.
Mohammed
Omar F
OF
Nibbering
Erik T J
ET
Dong
Jian
J
Solntsev
Kyril M
KM
Tolbert
Laren M
LM
D049452:Green Fluorescent Proteins / Q000737:chemistry*; D008164:Luminescent Proteins / Q000737:chemistry*; D011487:Protein Conformation; D013055:Spectrophotometry, Infrared
D008164:Luminescent Proteins; D049452:Green Fluorescent Proteins