ArticleProceedings of the National Academy of Sciences of the United States of America2009
Direct observation of an ensemble of stable collapsed states in the mechanical folding of ubiquitin.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 54 papers.
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Who cites it
54 citing papers in PubMed.
- Structure of a transient protein-folding intermediate by pressure-jump NMR spectroscopy.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Single-molecule magnetic tweezers to unravel protein folding dynamics under force.Biophysical reviews · 2025Review
- Direct observation of chaperone-modulated talin mechanics with single-molecule resolution.Communications biology · 2022Article
- Protein nanomechanics in biological context.Biophysical reviews · 2021Review
- Molecular Fluctuations as a Ruler of Force-Induced Protein Conformations.Nano letters · 2021Article
- Next Generation Methods for Single-Molecule Force Spectroscopy on Polyproteins and Receptor-Ligand Complexes.Frontiers in molecular biosciences · 2020Review
- Ephemeral states in protein folding under force captured with a magnetic tweezers design.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Nonnative Energetic Frustrations in Protein Folding at Residual Level: A Simulation Study of Homologous Immunoglobulin-likeInternational journal of molecular sciences · 2018Article
- The cohesin module is a major determinant of cellulosome mechanical stability.The Journal of biological chemistry · 2018Article
- Study of protein folding under native conditions by rapidly switching the hydrostatic pressure inside an NMR sample cell.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- The Work of Titin Protein Folding as a Major Driver in Muscle Contraction.Annual review of physiology · 2018Review
- The force-dependent mechanism of DnaK-mediated mechanical folding.Science advances · 2018Article
- Disulfide isomerization reactions in titin immunoglobulin domains enable a mode of protein elasticity.Nature communications · 2018Article
- Mechanically switching single-molecule fluorescence of GFP by unfolding and refolding.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Proteins Breaking Bad: A Free Energy Perspective.The journal of physical chemistry letters · 2017Article
- Force generation by titin folding.Protein science : a publication of the Protein Society · 2017Article
- Tailoring protein nanomechanics with chemical reactivity.Nature communications · 2017Article
- A HaloTag Anchored Ruler for Week-Long Studies of Protein Dynamics.Journal of the American Chemical Society · 2016Article
- Protein S-sulfenylation is a fleeting molecular switch that regulates non-enzymatic oxidative folding.Nature communications · 2016Article
- A simple two-state protein unfolds mechanically via multiple heterogeneous pathways at single-molecule resolution.Nature communications · 2016Article
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5 authors.
Funding
Abstract
Statistical theories of protein folding have long predicted plausible mechanisms for reducing the vast conformational space through distinct ensembles of structures. However, these predictions have remained untested by bulk techniques, because the conformational diversity of folding molecules has been experimentally unapproachable. Owing to recent advances in single molecule force-clamp spectroscopy, we are now able to probe the structure and dynamics of the small protein ubiquitin by measuring its length and mechanical stability during each stage of folding. Here, we discover that upon hydrophobic collapse, the protein rapidly selects a subset of minimum energy structures that are mechanically weak and essential precursors of the native fold. From this much reduced ensemble, the native state is acquired through a barrier-limited transition. Our results support the validity of statistical mechanics models in describing the folding of a small protein on biological timescales.
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