ArticleProtein science : a publication of the Protein Society2014
Green-lighting green fluorescent protein: faster and more efficient folding by eliminating a cis-trans peptide isomerization event.
Article in Protein science : a publication of the Protein Society, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed.
- Immobilization and enhancement of a heterodimeric fluorescence biosensor in fibrous protein biomaterials.Protein science : a publication of the Protein Society · 2025Article
- Non-invasive single cell aptasensing in live cells and animals.Chemical science · 2024Article
- Fast design of arbitrary length loops in proteins using InteractiveRosetta.BMC bioinformatics · 2018Article
- Mispacking and the Fitness Landscape of the Green Fluorescent Protein Chromophore Milieu.Biochemistry · 2017Article
- Toward Computationally Designed Self-Reporting Biosensors Using Leave-One-Out Green Fluorescent Protein.Biochemistry · 2015Article
- Exploring the folding pathway of green fluorescent protein through disulfide engineering.Protein science : a publication of the Protein Society · 2015Article
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Authors and funding
9 authors.
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Abstract
Wild-type green fluorescent protein (GFP) folds on a time scale of minutes. The slow step in folding is a cis-trans peptide bond isomerization. The only conserved cis-peptide bond in the native GFP structure, at P89, was remodeled by the insertion of two residues, followed by iterative energy minimization and side chain design. The engineered GFP was synthesized and found to fold faster and more efficiently than its template protein, recovering 50% more of its fluorescence upon refolding. The slow phase of folding is faster and smaller in amplitude, and hysteresis in refolding has been eliminated. The elimination of a previously reported kinetically trapped state in refolding suggests that X-P89 is trans in the trapped state. A 2.55 Å resolution crystal structure revealed that the new variant contains only trans-peptide bonds, as designed. This is the first instance of a computationally remodeled fluorescent protein that folds faster and more efficiently than wild type.
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