ArticleJournal of molecular biology2014
Microsecond barrier-limited chain collapse observed by time-resolved FRET and SAXS.
Article in Journal of molecular biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 48 citations in OpenAlex.
- Advances in microfluidic mixers for time-resolved structural biology with X-rays.Biophysical reviews · 2025Review
- Droplet Microfluidics for Food and Nutrition Applications.Micromachines · 2021Review
- A multi-step nucleation process determines the kinetics of prion-like domain phase separation.Nature communications · 2021Article
- Dramatic Shape Changes Occur as CytochromeThe journal of physical chemistry. B · 2020Article
- Friction-Limited Folding of Disulfide-Reduced Monomeric SOD1.Biophysical journal · 2020Article
- Water as a Good Solvent for Unfolded Proteins: Folding and Collapse are Fundamentally Different.Journal of molecular biology · 2020Review
- Nonnative structure in a peptide model of the unfolded state of superoxide dismutase 1 (SOD1): Implications for ALS-linked aggregation.The Journal of biological chemistry · 2019Article
- Frustration and folding of a TIM barrel protein.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Unfolded states under folding conditions accommodate sequence-specific conformational preferences with random coil-like dimensions.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Commonly used FRET fluorophores promote collapse of an otherwise disordered protein.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Local and non-local topological information in the denatured state ensemble of a β-barrel protein.Protein science : a publication of the Protein Society · 2018Article
- Unified understanding of folding and binding mechanisms of globular and intrinsically disordered proteins.Biophysical reviews · 2018Review
- Protein folding transition path times from single molecule FRET.Current opinion in structural biology · 2018Review
- Effect of an Imposed Contact on Secondary Structure in the Denatured State of Yeast Iso-1-cytochrome c.Biochemistry · 2017Article
- Innovative scattering analysis shows that hydrophobic disordered proteins are expanded in water.Science (New York, N.Y.) · 2017Article
- Simultaneous Determination of Two Subdomain Folding Rates Using the "Transfer-Quench" Method.Biophysical journal · 2017Article
- Perplexing cooperative folding and stability of a low-sequence complexity, polyproline 2 protein lacking a hydrophobic core.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- In Vitro Chromatin Assembly: Strategies and Quality Control.Methods in enzymology · 2016Article
- Methods for analysis of size-exclusion chromatography-small-angle X-ray scattering and reconstruction of protein scattering.Journal of applied crystallography · 2015Article
- Random coil negative control reproduces the discrepancy between scattering and FRET measurements of denatured protein dimensions.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
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Authors and funding
11 authors at 2 institutions in 1 country.
Funding
Abstract
It is generally held that random-coil polypeptide chains undergo a barrier-less continuous collapse when the solvent conditions are changed to favor the fully folded native conformation. We test this hypothesis by probing intramolecular distance distributions during folding in one of the paradigms of folding reactions, that of cytochrome c. The Trp59-to-heme distance was probed by time-resolved Förster resonance energy transfer in the microsecond time range of refolding. Contrary to expectation, a state with a Trp59-heme distance close to that of the guanidinium hydrochloride (GdnHCl) denatured state is present after ~27 μs of folding. A concomitant decrease in the population of this state and an increase in the population of a compact high-FRET (Förster resonance energy transfer) state (efficiency>90%) show that the collapse is barrier limited. Small-angle X-ray scattering (SAXS) measurements over a similar time range show that the radius of gyration under native favoring conditions is comparable to that of the GdnHCl denatured unfolded state. An independent comprehensive global thermodynamic analysis reveals that marginally stable partially folded structures are also present in the nominally unfolded GdnHCl denatured state. These observations suggest that specifically collapsed intermediate structures with low stability in rapid equilibrium with the unfolded state may contribute to the apparent chain contraction observed in previous fluorescence studies using steady-state detection. In the absence of significant dynamic averaging of marginally stable partially folded states and with the use of probes sensitive to distance distributions, barrier-limited chain contraction is observed upon transfer of the GdnHCl denatured state ensemble to native-like conditions.
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