ArticleBiochemistry2014
Ground-state proton transfer kinetics in green fluorescent protein.
Article in Biochemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
25 citing papers in PubMed, 66 citations in OpenAlex.
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- Localization and function of septins are susceptible to epitope tagging.bioRxiv : the preprint server for biology · 2025Article
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- Ranking Single Fluorescent Protein-Based Calcium Biosensor Performance by Molecular Dynamics Simulations.Journal of chemical information and modeling · 2025Article
- Localizations of the septin Spn4 tagged with GFP and mEGFP in fission yeast.microPublication biology · 2025Article
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- A genetically-encoded biosensor for direct detection of perfluorooctanoic acid.Scientific reports · 2023Article
- Structural origin and rational development of bright red noncanonical variants of green fluorescent protein.Physical chemistry chemical physics : PCCP · 2023Article
- Ratiometric Sensing of Redox Environments Inside Individual Carboxysomes Trapped in Solution.The journal of physical chemistry letters · 2022Article
- Unusual Spectroscopic and Electric Field Sensitivity of Chromophores with Short Hydrogen Bonds: GFP and PYP as Model Systems.The journal of physical chemistry. B · 2020Article
- Secondary structure effects on internal proton transfer in poly-peptides.Structural dynamics (Melville, N.Y.) · 2020Article
- A Not Obvious Correlation Between the Structure of Green Fluorescent Protein Chromophore Pocket and Hydrogen Bond Dynamics: A Choreography FromFrontiers in molecular biosciences · 2020Article
- NMR Reveals Light-Induced Changes in the Dynamics of a Photoswitchable Fluorescent Protein.Biophysical journal · 2019Article
- Kinetic and spectroscopic responses of pH-sensitive nanoparticles: influence of the silica matrix.RSC advances · 2019Article
- Unified Model for Photophysical and Electro-Optical Properties of Green Fluorescent Proteins.Journal of the American Chemical Society · 2019Article
- Understanding the Fluorescence Change in Red Genetically Encoded Calcium Ion Indicators.Biophysical journal · 2019Article
- Split Green Fluorescent Proteins: Scope, Limitations, and Outlook.Annual review of biophysics · 2019Review
- Photophysical Behavior of mNeonGreen, an Evolutionarily Distant Green Fluorescent Protein.Biophysical journal · 2018Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Proton transfer plays an important role in the optical properties of green fluorescent protein (GFP). While much is known about excited-state proton transfer reactions (ESPT) in GFP occurring on ultrafast time scales, comparatively little is understood about the factors governing the rates and pathways of ground-state proton transfer. We have utilized a specific isotopic labeling strategy in combination with one-dimensional (13)C nuclear magnetic resonance (NMR) spectroscopy to install and monitor a (13)C directly adjacent to the GFP chromophore ionization site. The chemical shift of this probe is highly sensitive to the protonation state of the chromophore, and the resulting spectra reflect the thermodynamics and kinetics of the proton transfer in the NMR line shapes. This information is complemented by time-resolved NMR, fluorescence correlation spectroscopy, and steady-state absorbance and fluorescence measurements to provide a picture of chromophore ionization reactions spanning a wide time domain. Our findings indicate that proton transfer in GFP is described well by a two-site model in which the chromophore is energetically coupled to a secondary site, likely the terminal proton acceptor of ESPT, Glu222. Additionally, experiments on a selection of GFP circular permutants suggest an important role played by the structural dynamics of the seventh β-strand in gating proton transfer from bulk solution to the buried chromophore.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.