ArticleProceedings of the National Academy of Sciences of the United States of America2008
The dual-basin landscape in GFP folding.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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Who cites it
31 citing papers in PubMed, 59 citations in OpenAlex.
- Catalyzing Protein Folding by Chaperones.Biology · 2025Review
- Evolving concepts of the protein universe.iScience · 2025Review
- Accessing isotopically labeled proteins containing genetically encoded phosphoserine for NMR with optimized expression conditions.The Journal of biological chemistry · 2022Article
- Magnesium controls aptamer-expression platform switching in the SAM-I riboswitch.Nucleic acids research · 2019Article
- Mispacking and the Fitness Landscape of the Green Fluorescent Protein Chromophore Milieu.Biochemistry · 2017Article
- Peculiarities of the Super-Folder GFP Folding in a Crowded Milieu.International journal of molecular sciences · 2016Article
- Wide-dynamic-range kinetic investigations of deep proton tunnelling in proteins.Nature chemistry · 2016Article
- Untangling the Influence of a Protein Knot on Folding.Biophysical journal · 2016Article
- Heterogeneous side chain conformation highlights a network of interactions implicated in hysteresis of the knotted protein, minimal tied trefoil.Journal of physics. Condensed matter : an Institute of Physics journal · 2015Article
- Exploring the balance between folding and functional dynamics in proteins and RNA.International journal of molecular sciences · 2015Article
- Geometrical Frustration in Interleukin-33 Decouples the Dynamics of the Functional Element from the Folding Transition State Ensemble.PloS one · 2015Article
- Differential contribution of tryptophans to the folding and stability of the attachment invasion locus transmembrane β-barrel from Yersinia pestis.Scientific reports · 2014Article
- Structural and dynamic changes associated with beneficial engineered single-amino-acid deletion mutations in enhanced green fluorescent protein.Acta crystallographica. Section D, Biological crystallography · 2014Article
- Random single amino acid deletion sampling unveils structural tolerance and the benefits of helical registry shift on GFP folding and structure.Structure (London, England : 1993) · 2014Article
- Pierced Lasso Bundles are a new class of knot-like motifs.PLoS computational biology · 2014Article
- Green-lighting green fluorescent protein: faster and more efficient folding by eliminating a cis-trans peptide isomerization event.Protein science : a publication of the Protein Society · 2014Article
- GFP variants with alternative β-strands and their application as light-driven protease sensors: a tale of two tails.Journal of the American Chemical Society · 2013Article
- Genetic incorporation of twelve meta-substituted phenylalanine derivatives using a single pyrrolysyl-tRNA synthetase mutant.ACS chemical biology · 2013Article
- Hysteresis as a Marker for Complex, Overlapping Landscapes in Proteins.The journal of physical chemistry letters · 2013Article
- Beta-barrel scaffold of fluorescent proteins: folding, stability and role in chromophore formation.International review of cell and molecular biology · 2013Review
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 1 country.
Funding
Abstract
Recent experimental studies suggest that the mature GFP has an unconventional landscape composed of an early folding event with a typical funneled landscape, followed by a very slow search and rearrangement step into the locked, active chromophore-containing structure. As we have shown previously, the substantial difference in time scales is what generates the observed hysteresis in thermodynamic folding. The interconversion between locked and the soft folding structures at intermediate denaturant concentrations is so slow that it is not observed under the typical experimental observation time. Simulations of a coarse-grained model were used to describe the fast folding event as well as identify native-like intermediates on energy landscapes enroute to the fluorescent native fold. Interestingly, these simulations reveal structural features of the slow dynamic transition to chromophore activation. Experimental evidence presented here shows that the trapped, native-like intermediate has structural heterogeneity in residues previously linked to chromophore formation. We propose that the final step of GFP folding is a "locking" mechanism leading to chromophore formation and high stability. The combination of previous experimental work and current simulation work is explained in the context of a dual-basin folding mechanism described above.
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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.