ArticleProceedings of the National Academy of Sciences of the United States of America2017
Mechanism and bottlenecks in strand photodissociation of split green fluorescent proteins (GFPs).
Article in Proceedings of the National Academy of Sciences of the United States of America, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 27 citations in OpenAlex.
- Dynamic assessment of PI4P metabolism using split GFP based sensors.Scientific reports · 2025Article
- Power Density Titration of Reversible Photoisomerization of a Fluorescent Protein Chromophore in the Presence of Thermally Driven Barrier Crossing Shown by Quantitative Millisecond Serial Synchrotron X-ray Crystallography.Journal of the American Chemical Society · 2024Article
- Engineering highly stable variants of Corynactis californica green fluorescent proteins.Protein science : a publication of the Protein Society · 2024Article
- Simulation-guided engineering of split GFPs with efficient β-strand photodissociation.Nature communications · 2023Article
- Energetic Basis and Design of Enzyme Function Demonstrated Using GFP, an Excited-State Enzyme.Journal of the American Chemical Society · 2022Article
- Internal conversion of the anionic GFP chromophore: in and out of the I-twisted SChemical science · 2022Article
- Engineering an efficient and bright split Corynactis californica green fluorescent protein.Scientific reports · 2021Article
- Electrostatic control of photoisomerization pathways in proteins.Science (New York, N.Y.) · 2020Article
- Unified Model for Photophysical and Electro-Optical Properties of Green Fluorescent Proteins.Journal of the American Chemical Society · 2019Article
- Development and Applications of Superfolder and Split Fluorescent Protein Detection Systems in Biology.International journal of molecular sciences · 2019Review
- Split Green Fluorescent Proteins: Scope, Limitations, and Outlook.Annual review of biophysics · 2019Review
- Structural Insight into the Photochemistry of Split Green Fluorescent Proteins: A Unique Role for a His-Tag.Journal of the American Chemical Society · 2018Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Split GFPs have been widely applied for monitoring protein-protein interactions by expressing GFPs as two or more constituent parts linked to separate proteins that only fluoresce on complementing with one another. Although this complementation is typically irreversible, it has been shown previously that light accelerates dissociation of a noncovalently attached β-strand from a circularly permuted split GFP, allowing the interaction to be reversible. Reversible complementation is desirable, but photodissociation has too low of an efficiency (quantum yield <1%) to be useful as an optogenetic tool. Understanding the physical origins of this low efficiency can provide strategies to improve it. We elucidated the mechanism of strand photodissociation by measuring the dependence of its rate on light intensity and point mutations. The results show that strand photodissociation is a two-step process involving light-activated
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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.