ArticleChemical physics2014
Structural Consequences of Chromophore Formation and Exploration of Conserved Lid Residues amongst Naturally Occurring Fluorescent Proteins.
Article in Chemical physics, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed, 8 citations in OpenAlex.
- Barrel Shape and Chromophore Rigidity Predict Fluorescent-Protein Photophysics.Journal of chemical information and modeling · 2026Article
- Design of a chromogenic substrate for elastase based on split GFP system-Proof of concept for colour switch sensors.Biotechnology reports (Amsterdam, Netherlands) · 2019Article
- Incomplete proteasomal degradation of green fluorescent proteins in the context of tandem fluorescent protein timers.Molecular biology of the cell · 2016Article
- GFP Loss-of-Function Mutations in Arabidopsis thaliana.G3 (Bethesda, Md.) · 2015Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
Abstract
Computational methods were used to generate the lowest energy conformations of the immature precyclized forms of the 28 naturally occurring GFP-like proteins deposited in the pdb. In all 28 GFP-like proteins, the beta-barrel contracts upon chromophore formation and becomes more rigid. Our prior analysis of over 260 distinct naturally occurring GFP-like proteins revealed that most of the conserved residues are located in the top and bottom of the barrel in the turns between the β-sheets.(1) Structural analyses, molecular dynamics simulations and the Anisotropic Network Model were used to explore the role of these conserved lid residues as possible folding nuclei. Our results are internally consistent and show that the conserved residues in the top and bottom lids undergo relatively less translational movement than other lid residues, and a number of these residues may play an important role as hinges or folding nuclei in the fluorescent proteins.
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Registered trials
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