ArticleJournal of molecular biology2008
Non-random-coil behavior as a consequence of extensive PPII structure in the denatured state.
Article in Journal of molecular biology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed.
- Protein folding stability estimation with explicit consideration of unfolded states.Nature communications · 2026Article
- Tuning the Dimensionality of Protein-Peptide Coassemblies to Build 2D Conductive Nanomaterials.ACS nano · 2025Article
- Unraveling the Mechanics of a Repeat-Protein Nanospring: From Folding of Individual Repeats to Fluctuations of the Superhelix.ACS nano · 2022Article
- Intrinsic Disorder in the T Cell Receptor Creates Cooperativity and Controls ZAP70 Binding.Biophysical journal · 2021Article
- Engineered protein-based functional nanopatterned materials for bio-optical devices.Nanoscale advances · 2019Article
- Adaptable hydrogel networks with reversible linkages for tissue engineering.Advanced materials (Deerfield Beach, Fla.) · 2015Review
- Cooperative recruitment of HMGB1 during V(D)J recombination through interactions with RAG1 and DNA.Nucleic acids research · 2013Article
- Article
- Modulating repeat protein stability: the effect of individual helix stability on the collective behavior of the ensemble.Protein science : a publication of the Protein Society · 2011Article
- Calorimetric study of a series of designed repeat proteins: modular structure and modular folding.Protein science : a publication of the Protein Society · 2011Article
- Stimuli-responsive smart gels realized via modular protein design.Journal of the American Chemical Society · 2010Article
- Denatured states of low-complexity polypeptide sequences differ dramatically from those of foldable sequences.Proceedings of the National Academy of Sciences of the United States of America · 2010Article
- Exploring the folding energy landscape of a series of designed consensus tetratricopeptide repeat proteins.Proceedings of the National Academy of Sciences of the United States of America · 2009Article
- Characterization of the unfolded state of repeat proteins.HFSP journal · 2008Article
- Structural landscape of the proline-rich domain of Sos1 nucleotide exchange factor.Biophysical chemistryArticle
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Authors and funding
6 authors.
Funding
Abstract
Unfolded proteins may contain a native or nonnative residual structure, which has important implications for the thermodynamics and kinetics of folding, as well as for misfolding and aggregation diseases. However, it has been universally accepted that residual structure should not affect the global size scaling of the denatured chain, which obeys the statistics of random coil polymers. Here we use a single-molecule optical technique--fluorescence correlation spectroscopy--to probe the denatured state of a set of repeat proteins containing an increasing number of identical domains, from 2 to 20. The availability of this set allows us to obtain the scaling law for the unfolded state of these proteins, which turns out to be unusually compact, strongly deviating from random coil statistics. The origin of this unexpected behavior is traced to the presence of an extensive nonnative polyproline II helical structure, which we localize to specific segments of the polypeptide chain. We show that the experimentally observed effects of polyproline II on the size scaling of the denatured state can be well-described by simple polymer models. Our findings suggest a hitherto unforeseen potential of nonnative structure to induce significant compaction of denatured proteins, significantly affecting folding pathways and kinetics.
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