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Updated: May 18, 2026

Examining the Conformational Dynamics of Membrane Proteins in situ with Site-directed Fluorescence Labeling
Published on: May 29, 2011
Site-selective hydrogen-bonding-induced fluorescence quenching of highly solvatofluorochromic GFP-like chromophores
Guan-Jhih Huang1, Jinn-Hsuan Ho, Ch Prabhakar
1Department of Chemistry, National Taiwan University, Taipei, Taiwan, 10617.
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.
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