Solvatochromism of the Green Fluorescence Protein Chromophore and Its Derivatives
Journal of the American Chemical Society2006Vol. 128(37), pp. 12038–12039
Citations Over TimeTop 10% of 2006 papers
Abstract
The solvatochromic behavior of the green fluorescence protein (GFP) chromophore (p-hydroxybenzylideneimidazolone, p-HBDI) and its derivatives (p-methoxybenzylideneimidazolone, p-MeOBDI, and N-methyl-p-hydroxybenzylideneimidazolonium iodide, p-HBDIMe+) was studied using UV−vis−absorption spectroscopy in a wide array of solvents. The relative contribution of specific (polarity) vs nonspecific (hydrogen-bonding) solvation to the absorbance spectra was studied. On the basis of these data, we discuss the nature of the absorption peak of the protonated and deprotonated forms of the wild-type GFP.
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