title: Excited-state structure determination of the green fluorescent protein chromophore.
abstract: 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.
authors.affiliation: Max Born Institut für Nichtlineare Optik und Kurzzeitspektroskopie, Max Born Strasse 2A, D-12489 Berlin, Germany.
authors.forename: Anwar
authors.initials: A
authors.lastname: Usman
authors.forename: Omar F
authors.initials: OF
authors.lastname: Mohammed
authors.forename: Erik T J
authors.initials: ET
authors.lastname: Nibbering
authors.forename: Jian
authors.initials: J
authors.lastname: Dong
authors.forename: Kyril M
authors.initials: KM
authors.lastname: Solntsev
authors.forename: Laren M
authors.initials: LM
authors.lastname: Tolbert
mesh_terms: D049452:Green Fluorescent Proteins / Q000737:chemistry*; D008164:Luminescent Proteins / Q000737:chemistry*; D011487:Protein Conformation; D013055:Spectrophotometry, Infrared
chemical_list: D008164:Luminescent Proteins; D049452:Green Fluorescent Proteins