title: Site-selective hydrogen-bonding-induced fluorescence quenching of highly solvatofluorochromic GFP-like chromophores.
abstract: The unconstrained green fluorescence protein (GFP)-like chromophore m-DMABDI displays a high solvatofluorochromicity in aprotic solvents, but the fluorescence is quenched in protic solvents. According to the site-specific intramolecularly hydrogen-bonded analogs 1OH and 2OH, the hydrogen bonding to the carbonyl oxygen is more important than that to the imino nitrogen of the imidazolinone group in the fluorescence quenching.
authors.affiliation: Department of Chemistry, National Taiwan University, Taipei, Taiwan, 10617.
authors.forename: Guan-Jhih
authors.initials: GJ
authors.lastname: Huang
authors.forename: Jinn-Hsuan
authors.initials: JH
authors.lastname: Ho
authors.forename: Ch
authors.initials: Ch
authors.lastname: Prabhakar
authors.forename: Yi-Hung
authors.initials: YH
authors.lastname: Liu
authors.forename: Shie-Ming
authors.initials: SM
authors.lastname: Peng
authors.forename: Jye-Shane
authors.initials: JS
authors.lastname: Yang
mesh_terms: D049452:Green Fluorescent Proteins / Q000737:chemistry*; D006860:Hydrogen Bonding; D015394:Molecular Structure; D012997:Solvents / Q000737:chemistry
chemical_list: D012997:Solvents; D049452:Green Fluorescent Proteins