ChemInform Abstract: Fluorescent Properties of Model Chromophores of Tyrosine‐66 Substituted Mutants of Aequorea Green Fluorescent Protein (GFP).

Abstract

Fluorescent Properties of Model Chromophores of Tyrosine-66 Substituted Mutants of Aequorea Green Fluorescent Protein (GFP). --(KOJIMA, S.; OHKAWA, H.; HIRANO, T.; MAKI, S.; NIWA, H.; OHASHI, M.; INOUYE, S.; TSUJI, F. I.; Tetrahedron Lett. 39 (1998) 29, 5239-5242; Dep. Appl. Phys. Chem., Univ. Electro-Commun., Chofu, Tokyo 182, Japan; EN)

The Effect of Conjugation on the Competition between Internal Conversion and Electron Detachment: A Comparison between Green Fluorescent and Red Kaede Protein Chromophores

“…1), is formed by the cyclisation and oxidation of Ser 65 -Tyr 66 -Gly 67 amino acid residues and is embedded within a β-barrel protein structure. 1,4,[7][8][9][10] The chromophore exists in deprotonated anionic (pHBDI -) or neutral forms and excitation of either of these leads to fluorescence from the deprotonated anionic chromophore at around 508 nm, with a quantum yield of Φ = 0.79 [11][12][13][14] (the neutral form deprotonates upon photoexcitation, yielding the anionic form). 11,15 An interesting feature of the isolated GFP chromophore is that it is non-fluorescent, in both solution and gasphases, 12,14,[16][17] as a result of efficient ultrafast non-radiative decay pathways being accessible in the absence of the protein.…”

Non-radiative relaxation dynamics of pyrrole following excitation in the range 249.5–200 nm

“…1), is formed by the cyclisation and oxidation of Ser 65 -Tyr 66 -Gly 67 amino acid residues and is embedded within a β-barrel protein structure. 1,4,[7][8][9][10] The chromophore exists in deprotonated anionic or neutral forms and excitation of either of these leads to fluorescence from the deprotonated anionic chromophore at around 508 nm, with a quantum yield of Φ = 0.79 [11][12][13][14] (the neutral form deprotonates upon photoexcitation, yielding the anionic form). 11,15 An interesting feature of the isolated GFP chromophore is that it is non-fluorescent, in both solution and gasphases, 12,14,[16][17] as a result of efficient ultrafast non-radiative decay pathways being accessible in the absence of the protein.…”

Enhanced EGFP Fluorescence Emission in Presence of PEG Aqueous Solutions andPIB1000-PEG6000-Muhammad1, Kryuchkova2, Dworeck3 et al. 2013BioMed Research International5000View full textAdd to dashboardCite

“…It is a 27 kDa protein, composed of 238 amino acids that are arranged in 11 antiparallel β -sheets forming β -barrel geometry. In the center of the β -barrel structure is located the covalently bound, p-hydroxybenzylidene-imidazolidinone based fluorophore [1] formed by a posttranslational autocatalytic cyclization of Ser-65, Tyr-66, and Gly-67 residues [2, 3]. This makes the GFP a flexible biological indicator and marker with broad applications; that is, GFP can be fused to a great number of proteins and allows their intracellular localization and detection [4].…”