Ab Initio Molecular Dynamics of the Green Fluorescent Protein (GFP) Chromophore:  An Insight into the Photoinduced Dynamics of Green Fluorescent Proteins

2001 ◽  
Vol 105 (24) ◽  
pp. 5797-5803 ◽  
Author(s):  
Valentina Tozzini ◽  
Riccardo Nifosì
Keyword(s):  
Molecular Dynamics ◽  
Green Fluorescent Protein ◽  
Ab Initio ◽  
Fluorescent Protein ◽  
Fluorescent Proteins ◽  
Ab Initio Molecular Dynamics ◽  
Green Fluorescent Proteins ◽  
Gfp Chromophore ◽  
Green Fluorescent ◽  
Insight Into

Against the NEER principle: The third type of photochromism for GFP chromophore derivatives

2021 ◽  
Author(s):  
Jun-Wei Liao ◽  
Robert Sung ◽  
Kuangsen Sung
Keyword(s):  
Excited State ◽  
Green Fluorescent Protein ◽  
Proton Transfer ◽  
Fluorescent Protein ◽  
Fluorescent Proteins ◽  
The Third ◽  
Excited State Proton Transfer ◽  
Gfp Chromophore ◽  
Green Fluorescent

Photochromism is the heart of photochromic fluorescent proteins. Excited-state proton transfer (ESPT) is the major photochromism for green fluorescent protein (GFP) and Z-E photoisomerization through τ-torsion is the major photochromism...

scholarly journals A photoactivatable green-fluorescent protein from the phylum Ctenophora

2009 ◽  
Vol 277 (1685) ◽  
pp. 1155-1160 ◽  
Author(s):  
Steven H. D. Haddock ◽  
Nadia Mastroianni ◽  
Lynne M. Christianson
Keyword(s):  
Green Fluorescent Protein ◽  
Fluorescent Protein ◽  
Fluorescent Proteins ◽  
Green Fluorescent Proteins ◽  
Optical Probes ◽  
Fluorescent Emission ◽  
The Family ◽  
Fluorescent State ◽  
Green Fluorescent

Genes for the family of green-fluorescent proteins (GFPs) have been found in more than 100 species of animals, with some species containing six or more copies producing a variety of colours. Thus far, however, these species have all been within three phyla: Cnidaria, Arthropoda and Chordata. We have discovered GFP-type fluorescent proteins in the phylum Ctenophora, the comb jellies. The ctenophore proteins share the x YG chromophore motif of all other characterized GFP-type proteins. These proteins exhibit the uncommon property of reversible photoactivation, in which fluorescent emission becomes brighter upon exposure to light, then gradually decays to a non-fluorescent state. In addition to providing potentially useful optical probes with novel properties, finding a fluorescent protein in one of the earliest diverging metazoans adds further support to the possibility that these genes are likely to occur throughout animals.

ELECTRONIC EXCITATIONS OF GREEN FLUORESCENT PROTEINS: MODELING SOLVATOCHROMATIC SHIFTS OF CHROMOPHORE MODEL COMPOUNDS IN SOLUTIONS

2006 ◽  
Vol 05 (spec01) ◽  
pp. 375-390 ◽  
Author(s):  
LIDONG ZHANG ◽  
DAIQIAN XIE ◽  
JUN ZENG
Keyword(s):  
Hydrogen Bonding ◽  
Fluorescent Protein ◽  
Fluorescent Proteins ◽  
Green Fluorescent Proteins ◽  
Many Body ◽  
Model Compounds ◽  
Reaction Field ◽  
Solvent Shifts ◽  
Gfp Chromophore ◽  
Green Fluorescent

Green fluorescent protein (GFP) is a spontaneously fluorescent protein due to its p-hydroxylbenzylideneimidazolidinone chromophore. In this work, we have investigated the electronic structures, liquid structures, and solvent shifts of the GFP chromophore model compounds 4′-hydroxylbenzylidene-2,3-dimethylimidazolin-5-one (HBDI) and 4′-hydroxylbenzylidene-2-methyl-imidazoin-5-one-3-acetate (HBMIA) in NaOH /aqueous solutions, in which both compounds are protonated at anionic state. The electronic structure calculations predict that both model compounds could adopt both cis and trans conformations in solutions. Moreover, liquid simulations elucidate an extensive well-defined hydrogen-bonding network between the solvent and the solute in the ground state. Furthermore, solvent shifts calculations indicate that contributions from the specific solute-solvent hydrogen-bonding interactions are negligible for the solvatochromatic shifts observed in the absorption spectrum of the model compounds in solutions; rather, the solvent shifts are dominated by the dipolar solvation in which both permanent charge–charge interactions and many-body polarizations contribute significantly. Self-Consistent Reaction-Field (SCRF) approach could be the efficient method for studying the unusual optical properties of the GFP chromophore in solutions and proteins.

Structural Evidence of Photoisomerization Pathways in Fluorescent Proteins

2019 ◽  
Author(s):  
Jeffrey Chang ◽  
Matthew Romei ◽  
Steven Boxer
Keyword(s):  
Rational Design ◽  
Fluorescent Protein ◽  
Fluorescent Proteins ◽  
Super Resolution ◽  
Unit Cell Size ◽  
Chlorine Substituent ◽  
Gfp Chromophore ◽  
The One ◽  
Green Fluorescent ◽  
Super Resolution Microscopy

<p>Double-bond photoisomerization in molecules such as the green fluorescent protein (GFP) chromophore can occur either via a volume-demanding one-bond-flip pathway or via a volume-conserving hula-twist pathway. Understanding the factors that determine the pathway of photoisomerization would inform the rational design of photoswitchable GFPs as improved tools for super-resolution microscopy. In this communication, we reveal the photoisomerization pathway of a photoswitchable GFP, rsEGFP2, by solving crystal structures of <i>cis</i> and <i>trans</i> rsEGFP2 containing a monochlorinated chromophore. The position of the chlorine substituent in the <i>trans</i> state breaks the symmetry of the phenolate ring of the chromophore and allows us to distinguish the two pathways. Surprisingly, we find that the pathway depends on the arrangement of protein monomers within the crystal lattice: in a looser packing, the one-bond-flip occurs, whereas in a tighter packing (7% smaller unit cell size), the hula-twist occurs.</p><p> </p><p> </p><p> </p><p> </p><p> </p><p> </p> <p> </p>

Fluorescent and “breathable” CO2 responsive vesicles inspired from green fluorescent protein

2017 ◽  
Vol 8 (40) ◽  
pp. 6283-6288 ◽  
Author(s):  
Lei Xu ◽  
Ning Ren ◽  
Ji Pang ◽  
Hongping Deng ◽  
Xinyuan Zhu ◽  
...  
Keyword(s):  
Green Fluorescent Protein ◽  
Block Copolymer ◽  
Fluorescent Protein ◽  
Gfp Chromophore ◽  
Green Fluorescent

CO2 responsive fluorescent vesicles from a GFP chromophore labeled block-copolymer could change their size and fluorescence to mimic jellyfish breathing.

scholarly journals Red-Shifted Aminated Derivatives of GFP Chromophore for Live-Cell Protein Labeling with Lipocalins

2018 ◽  
Vol 19 (12) ◽  
pp. 3778 ◽  
Author(s):  
Nina Bozhanova ◽  
Mikhail Baranov ◽  
Nadezhda Baleeva ◽  
Alexey Gavrikov ◽  
Alexander Mishin
Keyword(s):  
Green Fluorescent Protein ◽  
Live Cell Imaging ◽  
Cell Imaging ◽  
Fluorescent Protein ◽  
Live Cell ◽  
Protein Labeling ◽  
Cell Protein ◽  
Gfp Chromophore ◽  
Green Fluorescent ◽  
Derivatives Of

Fluorogens are an attractive type of dye for imaging applications, eliminating time-consuming washout steps from staining protocols. With just a handful of reported fluorogen-protein pairs, mostly in the green region of spectra, there is a need for the expansion of their spectral range. Still, the origins of solvatochromic and fluorogenic properties of the chromophores suitable for live-cell imaging are poorly understood. Here we report on the synthesis and labeling applications of novel red-shifted fluorogenic cell-permeable green fluorescent protein (GFP) chromophore analogs.

scholarly journals Single-Molecule Imaging and Computational Microscopy Approaches Clarify the Mechanism of the Dimerization and Membrane Interactions of Green Fluorescent Protein

2019 ◽  
Vol 20 (6) ◽  
pp. 1410 ◽  
Author(s):  
Xiaohua Wang ◽  
Kai Song ◽  
Yang Li ◽  
Ling Tang ◽  
Xin Deng
Keyword(s):  
Molecular Dynamics ◽  
Green Fluorescent Protein ◽  
Single Molecule ◽  
Fluorescent Protein ◽  
Hydrophobic Interactions ◽  
Site Directed Mutagenesis ◽  
Single Amino Acid ◽  
Single Mutation ◽  
Functional Protein ◽  
Green Fluorescent

Green fluorescent protein (GFP) is widely used as a biomarker in living systems; however, GFP and its variants are prone to forming low-affinity dimers under physiological conditions. This undesirable tendency is exacerbated when fluorescent proteins (FP) are confined to membranes, fused to naturally-oligomeric proteins, or expressed at high levels in cells. Oligomerization of FPs introduces artifacts into the measurement of subunit stoichiometry, as well as interactions between proteins fused to FPs. Introduction of a single mutation, A206K, has been shown to disrupt hydrophobic interactions in the region responsible for GFP dimerization, thereby contributing to its monomerization. Nevertheless, a detailed understanding of how this single amino acid-dependent inhibition of dimerization in GFP occurs at the atomic level is still lacking. Single-molecule experiments combined with computational microscopy (atomistic molecular dynamics) revealed that the amino group of A206 contributes to GFP dimer formation via a multivalent electrostatic interaction. We further showed that myristoyl modification is an efficient mechanism to promote membrane attachment of GFP. Molecular dynamics-based site-directed mutagenesis has been used to identify the key functional residues in FPs. The data presented here have been utilized as a monomeric control in downstream single-molecule studies, facilitating more accurate stoichiometry quantification of functional protein complexes in living cells.

Sign in / Sign up

Export Citation Format

Share Document