ArticleNature2007
A pre-existing hydrophobic collapse in the unfolded state of an ultrafast folding protein.
Article in Nature, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.
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Who cites it
51 citing papers in PubMed.
- DreamFold: A World Model to efficiently generate protein folding pathways in the latent space.Protein science : a publication of the Protein Society · 2026Article
- Nuclear-Spin Hyperpolarization of Biomolecules by Optically Enhanced NMR at Ultra-High Field.Journal of the Chinese Chemical Society. Zhongguo hua xue hui (Taipei, Taiwan) · 2026Article
- Article
- Continuous-Wave (CW) Photo-CIDNP NMR Spectroscopy: A Tutorial.Magnetic resonance in chemistry : MRC · 2025Article
- Photo-CIDNP of Solvent-Exposed Flavins in Flavoproteins.The journal of physical chemistry letters · 2025Article
- Importance of Inter-residue Contacts for Understanding Protein Folding and Unfolding Rates, Remote Homology, and Drug Design.Molecular biotechnology · 2025Review
- Protein Function Analysis through Machine Learning.Biomolecules · 2022Review
- Downhill, Ultrafast and Fast Folding Proteins Revised.International journal of molecular sciences · 2020Article
- Approximating dynamic proximity with a hybrid geometry energy-based kernel for diffusion maps.The Journal of chemical physics · 2019Article
- Collapse Transitions of Proteins and the Interplay Among Backbone, Sidechain, and Solvent Interactions.Annual review of biophysics · 2018Article
- Pushing nuclear magnetic resonance sensitivity limits with microfluidics and photo-chemically induced dynamic nuclear polarization.Nature communications · 2018Article
- Temperature evolution of Trp-cage folding pathways: An analysis by dividing the probability flux field into stream tubes.Journal of biological physics · 2017Article
- Experimental and Computational Analysis of Protein Stabilization by Gly-to-d-Ala Substitution: A Convolution of Native State and Unfolded State Effects.Journal of the American Chemical Society · 2016Article
- A hydrodynamic view of the first-passage folding of Trp-cage miniprotein.European biophysics journal : EBJ · 2016Article
- Fluorescein: A Photo-CIDNP Sensitizer Enabling Hypersensitive NMR Data Collection in Liquids at Low Micromolar Concentration.The journal of physical chemistry. B · 2016Article
- Nascent β-Hairpin Formation of a Natively Unfolded Peptide Reveals the Role of Hydrophobic Contacts.Biophysical journal · 2015Article
- Folding dynamics and pathways of the trp-cage miniproteins.Biochemistry · 2014Article
- Energetically significant networks of coupled interactions within an unfolded protein.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Role of tryptophan side chain dynamics on the Trp-cage mini-protein folding studied by molecular dynamics simulations.PloS one · 2014Article
- Circular Permutation of the Trp-cage: Fold Rescue upon Addition of a Hydrophobic Staple.RSC advances · 2013Article
Corrections and comments
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Authors and funding
7 authors.
Funding
Abstract
Insights into the conformational passage of a polypeptide chain across its free energy landscape have come from the judicious combination of experimental studies and computer simulations. Even though some unfolded and partially folded proteins are now known to possess biological function or to be involved in aggregation phenomena associated with disease states, experimentally derived atomic-level information on these structures remains sparse as a result of conformational heterogeneity and dynamics. Here we present a technique that can provide such information. Using a 'Trp-cage' miniprotein known as TC5b (ref. 5), we report photochemically induced dynamic nuclear polarization NMR pulse-labelling experiments that involve rapid in situ protein refolding. These experiments allow dipolar cross-relaxation with hyperpolarized aromatic side chain nuclei in the unfolded state to be identified and quantified in the resulting folded-state spectrum. We find that there is residual structure due to hydrophobic collapse in the unfolded state of this small protein, with strong inter-residue contacts between side chains that are relatively distant from one another in the native state. Prior structuring, even with the formation of non-native rather than native contacts, may be a feature associated with fast folding events in proteins.
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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.