Microelectronic circuit emulating Hydrogen Bonding Network of Green Fluorescent Protein

2016 ◽  
Author(s):  
Rostislav Pavlov Rusev ◽  
George Vasilev Angelov ◽  
Elitsa Emilova Gieva ◽  
Boris Petkov Atanasov ◽  
Marin Hristov Hristov
Keyword(s):  
Hydrogen Bonding ◽  
Green Fluorescent Protein ◽  
Fluorescent Protein ◽  
Hydrogen Bonding Network ◽  
Green Fluorescent

scholarly journals Role of Hydrogen Bonding in Green Fluorescent Protein-like Chromophore Emission

2019 ◽  
Vol 9 (1) ◽  
Author(s):  
Li Yang ◽  
Shifeng Nian ◽  
Guozhen Zhang ◽  
Edward Sharman ◽  
Hui Miao ◽  
...  
Keyword(s):  
Hydrogen Bonding ◽  
Green Fluorescent Protein ◽  
Fluorescent Protein ◽  
Green Fluorescent

scholarly journals The role of the tight-turn, broken hydrogen bonding, Glu222 and Arg96 in the post-translational green fluorescent protein chromophore formation

2008 ◽  
Vol 348 (1-3) ◽  
pp. 152-160 ◽  
Author(s):  
Nathan P. Lemay ◽  
Alicia L. Morgan ◽  
Elizabeth J. Archer ◽  
Luisa A. Dickson ◽  
Colleen M. Megley ◽  
...  
Keyword(s):  
Hydrogen Bonding ◽  
Green Fluorescent Protein ◽  
Fluorescent Protein ◽  
Green Fluorescent

Excited-State Proton Transfer in Fluorescent Photoactive Yellow Protein Containing 7-Hydroxycoumarin

2014 ◽  
Vol 896 ◽  
pp. 85-88
Author(s):  
Dian Novitasari ◽  
Hironari Kamikubo ◽  
Yoichi Yamazaki ◽  
Mariko Yamaguchi ◽  
Mikio Kataoka
Keyword(s):  
Hydrogen Bonding ◽  
Excited State ◽  
Proton Transfer ◽  
Fluorescent Protein ◽  
Stokes Shift ◽  
Spectroscopic Studies ◽  
Photoactive Yellow Protein ◽  
Excited State Proton Transfer ◽  
Hydrogen Bonding Network ◽  
Green Fluorescent

Green fluorescent protein (GFP) has been used as an effective tool in various biological fields. The large Stokes shift resulting from an excited-state proton transfer (ESPT) is the basis for the application of GFP in such techniques as ratiometric GFP biosensors. The chromophore of GFP is known to be involved in a hydrogen-bonding network. Previous X-ray crystallographic and FTIR studies suggest that a proton wire along the hydrogen-bonding network plays a role in the ESPT. In order to examine the relationship between the ESPT and hydrogen-bonding network within proteins, we prepared an artificial fluorescent protein using a light-sensor protein, photoactive yellow protein (PYP). The native chromophore of p-coumaric acid (pCA) of PYP undergoes trans-cis isomerization after absorbing a photon, which triggers proton transfers within the hydrogen-bonding network comprised of pCA and proximal amino acid residues. Although PYP emits little fluorescence, we succeeded to reconstitute an artificial fluorescent PYP (PYP-coumarin) by substituting the pCA with its trans-lock analog 7-hydroxycoumarin. Spectroscopic studies with PYP-coumarin revealed that the chromophore takes an anionic form at neutral pH, but is protonated by lowering pH. Both the protonated and deprotonated forms of PYP-coumarin emit intense fluorescence, as compared with the native PYP. In addition, both the deprotonated and protonated forms show identical λmax values in their fluorescence spectra, indicating that ESPT occurs in the artificial fluorescent protein.

Topochemistry and Photomechanical Effects in Crystals of Green Fluorescent Protein-like Chromophores: Effects of Hydrogen Bonding and Crystal Packing

2010 ◽  
Vol 132 (16) ◽  
pp. 5845-5857 ◽  
Author(s):  
Panče Naumov ◽  
Janusz Kowalik ◽  
Kyril M. Solntsev ◽  
Anthony Baldridge ◽  
Jong-Seok Moon ◽  
...  
Keyword(s):  
Hydrogen Bonding ◽  
Green Fluorescent Protein ◽  
Fluorescent Protein ◽  
Crystal Packing ◽  
Green Fluorescent
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