ArticleProceedings of the National Academy of Sciences of the United States of America2004
Random-coil behavior and the dimensions of chemically 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. An erratum has been issued. Cited by 332 papers.
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332 citing papers in PubMed.
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- In Search of Shape in the Unshaped: Constructing Ensembles of Intrinsically Disordered Proteins.Biophysics reviews · 2026Article
- Human Endothelial Membrane as a Structural Prototype: A Comparative Analysis withInternational journal of molecular sciences · 2026Article
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- Manipulating the Unfolded State of a Folded Protein through Site-Specific Backbone Modification.Biochemistry · 2026Article
- Protein folding stability estimation with explicit consideration of unfolded states.Nature communications · 2026Article
- Accurate prediction of thermoresponsive phase behavior of disordered proteins.Protein science : a publication of the Protein Society · 2025Article
- Cahn-Hilliard dynamical models for condensed biomolecular systems.bioRxiv : the preprint server for biology · 2025Article
- Sizes, conformational fluctuations, and SAXS profiles for intrinsically disordered proteins.Protein science : a publication of the Protein Society · 2025Article
- Assembly Formation of P65 Protein, Featured by an Intrinsically Disordered Region Involved in Gliding Machinery ofBiomolecules · 2025Article
- Accurate prediction of thermoresponsive phase behavior of disordered proteins.bioRxiv : the preprint server for biology · 2025Article
- ATP promotes protein coacervation through conformational compaction.Journal of molecular cell biology · 2025Article
- Synthesis of Novel Indolyl Aryl Sulfone-clubbed Hydrazone Derivatives as Potential HIV-1 Non-Nucleoside Reverse Transcriptase Inhibitors: Molecular Modeling and QSAR Studies.Current medicinal chemistry · 2025Article
- Blobs form during the single-file transport of proteins across nanopores.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- CD28 hinge used in chimeric antigen receptor (CAR) T-cells exhibits local structure and conformational exchange amidst global disorder.Communications biology · 2024Article
272 more citing papers are in PubMed but not listed here.
Corrections and comments
- Erratum issued
Authors and funding
15 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Spectroscopic studies have identified a number of proteins that appear to retain significant residual structure under even strongly denaturing conditions. Intrinsic viscosity, hydrodynamic radii, and small-angle x-ray scattering studies, in contrast, indicate that the dimensions of most chemically denatured proteins scale with polypeptide length by means of the power-law relationship expected for random-coil behavior. Here we further explore this discrepancy by expanding the length range of characterized denatured-state radii of gyration (R(G)) and by reexamining proteins that reportedly do not fit the expected dimensional scaling. We find that only 2 of 28 crosslink-free, prosthetic-group-free, chemically denatured polypeptides deviate significantly from a power-law relationship with polymer length. The R(G) of the remaining 26 polypeptides, which range from 16 to 549 residues, are well fitted (r(2) = 0.988) by a power-law relationship with a best-fit exponent, 0.598 +/- 0.028, coinciding closely with the 0.588 predicted for an excluded volume random coil. Therefore, it appears that the mean dimensions of the large majority of chemically denatured proteins are effectively indistinguishable from the mean dimensions of a random-coil ensemble.
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