ArticleProceedings of the National Academy of Sciences of the United States of America2013
Toward an atomistic description of the urea-denatured state of proteins.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed.
- Site-Specific Antigen Immobilization Improves Autoantibody Binding Efficiency on the Luminex Platform.ACS omega · 2026Article
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- Tailoring Peptide Coacervates for Advanced Biotechnological Applications: Enhancing Control, Encapsulation, and Antioxidant Properties.ACS applied materials & interfaces · 2025Article
- Structural Context Modulates the Conformational Ensemble of the Intrinsically Disordered Amino Terminus of α-Synuclein.Journal of the American Chemical Society · 2025Article
- Structural basis of urea transport by Arabidopsis thaliana DUR3.Nature communications · 2025Article
- Colorimetric Detection of Bovine Serum Albumin (BSA Protein) by Interaction and Modification of Silver Nanoparticles.ACS omega · 2025Article
- Dry molten globule conformational state of CYP11A1 (SCC) regulates the first step of steroidogenesis in the mitochondrial matrix.iScience · 2024Article
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- Correlation between chemical denaturation and the unfolding energetics of Acanthamoeba actophorin.Biophysical journal · 2023Article
- Expression, purification, and characterisation of the p53 binding domain of Retinoblastoma binding protein 6 (RBBP6).PloS one · 2023Article
- DMSO-Quenched H/D-Exchange 2D NMR Spectroscopy and Its Applications in Protein Science.Molecules (Basel, Switzerland) · 2022Review
- Protein Unfolding: Denaturant vs. Force.Biomedicines · 2021Article
- Residual Structure of Unfolded Ubiquitin as Revealed by Hydrogen/Deuterium-Exchange 2D NMR.Biophysical journal · 2020Article
- Article
- Article
- Conditionally disordered proteins: bringing the environment back into the fold.Cellular and molecular life sciences : CMLS · 2017Review
- Protein unfolding mechanisms and their effects on folding experiments.F1000Research · 2017Review
- Tau Aggregation Propensity Engrained in Its Solution State.The journal of physical chemistry. B · 2015Article
- Influence of chemical denaturants on the activity, fold and zinc status of anthrax lethal factor.Biochemistry and biophysics reports · 2015Article
- Exploring the role of receptor flexibility in structure-based drug discovery.Biophysical chemistry · 2014Review
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Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
We present here the characterization of the structural, dynamics, and energetics of properties of the urea-denatured state of ubiquitin, a small prototypical soluble protein. By combining state-of-the-art molecular dynamics simulations with NMR and small-angle X-ray scattering data, we were able to: (i) define the unfolded state ensemble, (ii) understand the energetics stabilizing unfolded structures in urea, (iii) describe the dedifferential nature of the interactions of the fully unfolded proteins with urea and water, and (iv) characterize the early stages of protein refolding when chemically denatured proteins are transferred to native conditions. The results presented herein are unique in providing a complete picture of the chemically unfolded state of proteins and contribute to deciphering the mechanisms that stabilize the native state of proteins, as well as those that maintain them unfolded in the presence of urea.
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