ArticleProceedings of the National Academy of Sciences of the United States of America2008
Protein folding: independent unrelated pathways or predetermined pathway with optional errors.
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 20 papers.
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Who cites it
20 citing papers in PubMed.
- Pore formation by the CDTb component of the Clostridioides difficile binary toxin is CaCommunications biology · 2025Article
- Protein folding in vitro and in the cell: From a solitary journey to a team effort.Biophysical chemistry · 2022Review
- Stability of uniformly labeled (Scientific reports · 2021Article
- Life in Phases: Intra- and Inter- Molecular Phase Transitions in Protein Solutions.Biomolecules · 2019Review
- Novel Kinetic Intermediates Populated along the Folding Pathway of the Transmembrane β-Barrel OmpA.Biochemistry · 2017Article
- How cooperative are protein folding and unfolding transitions?Protein science : a publication of the Protein Society · 2016Review
- The nature of protein folding pathways.Proceedings of the National Academy of Sciences of the United States of America · 2014Review
- Conditionally and transiently disordered proteins: awakening cryptic disorder to regulate protein function.Chemical reviews · 2014Review
- Folding of a large protein at high structural resolution.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Under-folded proteins: Conformational ensembles and their roles in protein folding, function, and pathogenesis.Biopolymers · 2013Article
- Hypothetical in silico model of the early-stage intermediate in protein folding.Journal of molecular modeling · 2013Article
- Stepwise protein folding at near amino acid resolution by hydrogen exchange and mass spectrometry.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- β-hairpin forms by rolling up from C-terminal: topological guidance of early folding dynamics.Scientific reports · 2012Article
- Quantitative assessment of protein structural models by comparison of H/D exchange MS data with exchange behavior accurately predicted by DXCOREX.Journal of the American Society for Mass Spectrometry · 2012Article
- Folding mechanism of β-hairpin trpzip2: heterogeneity, transition state and folding pathways.International journal of molecular sciences · 2009Review
- Discrete-continuous duality of protein structure space.Current opinion in structural biology · 2009Review
- Folding by numbers: primary sequence statistics and their use in studying protein folding.International journal of molecular sciences · 2009Review
- Intra-molecular chaperone: the role of the N-terminal in conformational selection and kinetic control.Physical biology · 2009Article
- How main-chains of proteins explore the free-energy landscape in native states.Proceedings of the National Academy of Sciences of the United States of America · 2008Article
- The spectrum of biomolecular states and motions.HFSP journal · 2008Article
Corrections and comments
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Authors and funding
4 authors.
Funding
Abstract
The observation of heterogeneous protein folding kinetics has been widely interpreted in terms of multiple independent unrelated pathways (IUP model), both experimentally and in theoretical calculations. However, direct structural information on folding intermediates and their properties now indicates that all of a protein population folds through essentially the same stepwise pathway, determined by cooperative native-like foldon units and the way that the foldons fit together in the native protein. It is essential to decide between these fundamentally different folding mechanisms. This article shows, contrary to previous supposition, that the heterogeneous folding kinetics observed for the staphylococcal nuclease protein (SNase) does not require alternative parallel pathways. SNase folding kinetics can be fit equally well by a single predetermined pathway that allows for optional misfolding errors, which are known to occur ubiquitously in protein folding. Structural, kinetic, and thermodynamic information for the folding intermediates and pathways of many proteins is consistent with the predetermined pathway-optional error (PPOE) model but contrary to the properties implied in IUP models.
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