منابع مشابه
The thermal isomerization of the GFP chromophore: A computational study.
We present a density functional theory (B3LYP) study of the isomerization of 4-hydroxybenzylidene-1,2-dimethyl-imidazolinone (HOBDI), which is to mimic the green fluorescent protein (GFP) chromophore, in the ground state promoted by a nucleophile. Four solvents with different polarity, water, DMSO, methanol, and benzene, have been used to characterize the nucleophile assisted mechanism. The for...
متن کاملChemically modulating the photophysics of the GFP chromophore.
There is growing interest in engineering the properties of fluorescent proteins through modifications to the chromophore structure utilizing mutagenesis with either natural or unnatural amino acids. This entails an understanding of the photophysical and photochemical properties of the modified chromophore. In this work, a range of GFP chromophores with different alkyl substituents are synthesiz...
متن کاملPhotoelectron spectroscopy of the model GFP chromophore anion.
A photoelectron spectroscopy study of the anionic model chromophore of the green fluorescent protein is presented. From the photoelectron spectra taken at 3.496 eV, 4.62 eV, and 6.15 eV the vertical and adiabatic detachment energies are determined to be 2.8 ± 0.1 eV and 2.6 ± 0.2 eV, respectively. The vertical detachment energy is higher than the S1← S0 absorption maximum (2.57 eV) and indicate...
متن کاملThe hole in the barrel: water exchange at the GFP chromophore.
Internal water molecules in proteins are conceivably part of the protein structure, not exchanging easily with the bulk. We present a detailed molecular dynamics study of the water molecule bound to the green fluorescent protein (GFP) chromophore that conducts its proton following photoexcitation. It readily exchanges above 310 K through a hole that forms between strands 7 and 10, due to fluctu...
متن کاملHow far can a single hydrogen bond tune the spectral properties of the GFP chromophore?
Photoabsorption of the hydrogen-bonded complex of a neutral and an anionic Green Fluorescent Protein chromophore has been studied using a new dual-detection approach to action-absorption spectroscopy. Following absorption of one photon, dissociation through a single channel ensures that the full absorption spectrum is measured. Our theoretical account of the spectral shape reveals that the anio...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 2005
ISSN: 0021-9258
DOI: 10.1074/jbc.c400484200