ArticleJournal of physics. Condensed matter : an Institute of Physics journal2007
Folding and unfolding of a non-fluorescent mutant of green fluorescent protein.
Article in Journal of physics. Condensed matter : an Institute of Physics journal, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 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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Who cites it
9 citing papers in PubMed.
- Live-cell co-translational folding tracking reveals bidirectional coupling between translation and folding.bioRxiv : the preprint server for biology · 2026Article
- Shifting the balance: soluble ADAM10 as a potential treatment for Alzheimer's disease.Frontiers in aging neuroscience · 2023Article
- An Autonomous Molecular Bioluminescent Reporter (AMBER) for Voltage Imaging in Freely Moving Animals.Advanced biology · 2021Article
- Reductional Meiosis I Chromosome Segregation Is Established by Coordination of Key Meiotic Kinases.Developmental cell · 2019Article
- Genetically encoded optochemical probes for simultaneous fluorescence reporting and light activation of protein function with two-photon excitation.Journal of the American Chemical Society · 2014Article
- Beta-barrel scaffold of fluorescent proteins: folding, stability and role in chromophore formation.International review of cell and molecular biology · 2013Review
- Article
- Self-assembly of soft nanoparticles with tunable patchiness.Nature nanotechnology · 2009Article
- The dual-basin landscape in GFP folding.Proceedings of the National Academy of Sciences of the United States of America · 2008Article
Corrections and comments
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Authors and funding
5 authors.
Funding
Abstract
Green fluorescent protein (GFP), from the Pacific jellyfish A. victoria, has numerous uses in biotechnology and cell and molecular biology as a protein marker because of its specific chromophore, which is spontaneously created after proper protein folding. After formation, the chromophore is very stable and remains intact during protein unfolding, meaning that the GFP unfolding process is not the reverse of the original folding reaction; i.e., the principles of microscopic reversibility do not apply. We have generated the mutant S65T/G67A-GFP, which is unable to form the cyclic chromophore, with the goal of investigating the folding, unfolding and competing aggregation of GFP under fully reversible conditions. Our studies have been performed in the presence of GdnHCl. The GFP conformation was monitored using intrinsic tryptophan fluorescence, and fluorescence of bis-ANS. Light scattering was used to follow GFP aggregation. We conclude from these fluorescence measurements, that S65T/G67A-GFP folding is largely reversible. During equilibrium folding, the first step is formation of molten globule, prone to aggregation.
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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.