ArticleProtein science : a publication of the Protein Society2010
Urea denatured state ensembles contain extensive secondary structure that is increased in hydrophobic proteins.
Article in Protein science : a publication of the Protein Society, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed.
- Manipulating the Unfolded State of a Folded Protein through Site-Specific Backbone Modification.Biochemistry · 2026Article
- Sequential backbone chemical shift assignments of a cancer-associated isoform of the HBx protein from human hepatitis B virus.Biomolecular NMR assignments · 2025Article
- Optimization of protein-level tandem mass tag (TMT) labeling conditions in complex samples with top-down proteomics.Analytica chimica acta · 2022Article
- Iris: Interactive all-in-one graphical validation of 3D protein model iterations.Protein science : a publication of the Protein Society · 2021Article
- 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
- Production and characterization of a thermostable antifungal chitinase secreted by the filamentous fungus3 Biotech · 2018Article
- Lectin- and Saccharide-Functionalized Nano-Chemiresistor Arrays for Detection and Identification of Pathogenic Bacteria Infection.Biosensors · 2018Article
- Denaturation and Aggregation of Interferon-τ in Aqueous Solution.Pharmaceutical research · 2018Article
- Rapid quantitative analysis of monoclonal antibody heavy and light chain charge heterogeneity.mAbs · 2015Article
- Contribution of hydrogen bonds to protein stability.Protein science : a publication of the Protein Society · 2014Article
- Urea-temperature phase diagrams capture the thermodynamics of denatured state expansion that accompany protein unfolding.Protein science : a publication of the Protein Society · 2013Article
- Membrane protein thermodynamic stability may serve as the energy sink for sorting in the periplasm.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- In vivo detection and quantification of chemicals that enhance protein stability.Analytical biochemistry · 2013Article
- Small-angle X-ray scattering and single-molecule FRET spectroscopy produce highly divergent views of the low-denaturant unfolded state.Journal of molecular biology · 2012Article
- Residual structure in unfolded proteins.Current opinion in structural biology · 2012Review
- Osmolyte effects on protein stability and solubility: a balancing act between backbone and side-chains.Biophysical chemistry · 2011Article
- How do thermophilic proteins and proteomes withstand high temperature?Biophysical journal · 2011Article
- Contribution of hydrophobic interactions to protein stability.Journal of molecular biology · 2011Article
- The CLN025 decapeptide retains a β-hairpin conformation in urea and guanidinium chloride.The journal of physical chemistry. B · 2011Article
- Counting peptide-water hydrogen bonds in unfolded proteins.Protein science : a publication of the Protein Society · 2011Article
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6 authors.
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Abstract
The goal of this article is to gain a better understanding of the denatured state ensemble (DSE) of proteins through an experimental and computational study of their denaturation by urea. Proteins unfold to different extents in urea and the most hydrophobic proteins have the most compact DSE and contain almost as much secondary structure as folded proteins. Proteins that unfold to the greatest extent near pH 7 still contain substantial amounts of secondary structure. At low pH, the DSE expands due to charge-charge interactions and when the net charge per residue is high, most of the secondary structure is disrupted. The proteins in the DSE appear to contain substantial amounts of polyproline II conformation at high urea concentrations. In all cases considered, including staph nuclease, the extent of unfolding by urea can be accounted for using the data and approach developed in the laboratory of Wayne Bolen (Auton et al., Proc Natl Acad Sci 2007; 104:15317-15323).
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