ArticleProceedings of the National Academy of Sciences of the United States of America2004
Reassessing random-coil statistics in unfolded proteins.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 157 papers.
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157 citing papers in PubMed.
- Chain collapse, reduced dielectric, and water release drive protein phase separation.Biophysical journal · 2026Article
- Hydrogen-exchange behavior of the L20A mutant of the protein A B domain in guanidinium chloride: evidence for persistent native-like contacts.Scientific reports · 2026Article
- Nearest neighbour interactions between amino acid residues in short peptides and coil libraries.RSC advances · 2026Article
- The filamentous ultrastructure of the PopZ condensate is required for its cellular function.Nature structural & molecular biology · 2026Article
- First report of novel single nucleotide polymorphisms (SNPs) and genetic characteristics of the prion-like protein gene (Frontiers in veterinary science · 2026Article
- Direct Optical Quantification of Chain Collapse, Reduced Dielectric, and Water Release Driving Protein Phase Separation.bioRxiv : the preprint server for biology · 2025Article
- Industrial-scale fractionation of fava bean, chickpea, and red lentil: A comparative analysis of composition, antinutrients, nutrition, structure, and functionality.Current research in food science · 2025Article
- A Hydrophobic Core Stabilizes the Residual Structure in the RRM2 Intermediate State of the ALS-linked Protein TDP-43.Journal of molecular biology · 2024Article
- Protein Binding Leads to Reduced Stability and Solvated Disorder in the Polystyrene Nanoparticle Corona.Small (Weinheim an der Bergstrasse, Germany) · 2024Article
- Ensemble structure of the N-terminal domain (1-267) of FUS in a biomolecular condensate.Biophysical journal · 2024Article
- An amino-domino model described by a cross-peptide-bond Ramachandran plot defines amino acid pairs as local structural units.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Generation of unfolded outer membrane protein ensembles defined by hydrodynamic properties.European biophysics journal : EBJ · 2023Article
- Intrinsically disordered regions that drive phase separation form a robustly distinct protein class.The Journal of biological chemistry · 2023Article
- Structural properties of the HNF-1A transactivation domain.Frontiers in molecular biosciences · 2023Article
- Measuring the Radius of Gyration and Intrinsic Flexibility of Viral Proteins in Buffer Solution Using Small-Angle X-ray Scattering.ACS measurement science au · 2022Article
- Integration of Nanometer-Range Label-to-Label Distances and Their Distributions into Modelling Approaches.Biomolecules · 2022Review
- New insights into the folding-unfolding mechanism and conformations of cytochrome C.Chemical science · 2022Article
- Exploring Nearest Neighbor Interactions and Their Influence on the Gibbs Energy Landscape of Unfolded Proteins and Peptides.International journal of molecular sciences · 2022Review
- Molecular mechanisms underlying the role of the centriolar CEP164-TTBK2 complex in ciliopathies.Structure (London, England : 1993) · 2022Article
- Is Protein Folding a Thermodynamically Unfavorable, Active, Energy-Dependent Process?International journal of molecular sciences · 2022Review
97 more citing papers are in PubMed but not listed here.
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2 authors.
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Abstract
The Gaussian-distributed random coil has been the dominant model for denatured proteins since the 1950s, and it has long been interpreted to mean that proteins are featureless, statistical coils in 6 M guanidinium chloride. Here, we demonstrate that random-coil statistics are not a unique signature of featureless polymers. The random-coil model does predict the experimentally determined coil dimensions of denatured proteins successfully. Yet, other equally convincing experiments have shown that denatured proteins are biased toward specific conformations, in apparent conflict with the random-coil model. We seek to resolve this paradox by introducing a contrived counterexample in which largely native protein ensembles nevertheless exhibit random-coil characteristics. Specifically, proteins of known structure were used to generate disordered conformers by varying backbone torsion angles at random for approximately 8% of the residues; the remaining approximately 92% of the residues remained fixed in their native conformation. Ensembles of these disordered structures were generated for 33 proteins by using a torsion-angle Monte Carlo algorithm with hard-sphere sterics; bulk statistics were then calculated for each ensemble. Despite this extreme degree of imposed internal structure, these ensembles have end-to-end distances and mean radii of gyration that agree well with random-coil expectations in all but two cases.
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