ArticleBiophysical journal2009
Urea impedes the hydrophobic collapse of partially unfolded proteins.
Article in Biophysical journal, 2009. 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, 74 citations in OpenAlex.
- Piecewise All-Atom SMD Simulations Reveal Key Secondary Structures in Luciferase Unfolding Pathway.Biophysical journal · 2020Article
- Urea-aromatic interactions in biology.Biophysical reviews · 2020Review
- Denaturation and Aggregation of Interferon-τ in Aqueous Solution.Pharmaceutical research · 2018Article
- Structure and dynamics of urea/water mixtures investigated by vibrational spectroscopy and molecular dynamics simulation.The journal of physical chemistry. B · 2013Article
- Toward an atomistic description of the urea-denatured state of proteins.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Using simulations to provide the framework for experimental protein folding studies.Archives of biochemistry and biophysics · 2013Review
- Exploring early stages of the chemical unfolding of proteins at the proteome scale.PLoS computational biology · 2013Article
- Quantitative characterization of local protein solvation to predict solvent effects on protein structure.Biophysical journal · 2012Article
- Article
- The CLN025 decapeptide retains a β-hairpin conformation in urea and guanidinium chloride.The journal of physical chemistry. B · 2011Article
- Comment on "urea-mediated protein denaturation: a consensus view".The journal of physical chemistry. B · 2011Article
- Interaction of β-sheet folds with a gold surface.PloS one · 2011Article
- Role of solvation effects in protein denaturation: from thermodynamics to single molecules and back.Annual review of physical chemistry · 2011Review
- Stability of protein pharmaceuticals: an update.Pharmaceutical research · 2010Review
- Native state dynamics drive the unfolding of the SH3 domain of PI3 kinase at high denaturant concentration.Proceedings of the National Academy of Sciences of the United States of America · 2009Article
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Authors and funding
2 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Proteins are denatured in aqueous urea solution. The nature of the molecular driving forces has received substantial attention in the past, whereas the question how urea acts at different phases of unfolding is not yet well understood at the atomic level. In particular, it is unclear whether urea actively attacks folded proteins or instead stabilizes unfolded conformations. Here we investigated the effect of urea at different phases of unfolding by molecular dynamics simulations, and the behavior of partially unfolded states in both aqueous urea solution and in pure water was compared. Whereas the partially unfolded protein in water exhibited hydrophobic collapses as primary refolding events, it remained stable or even underwent further unfolding steps in aqueous urea solution. Further, initial unfolding steps of the folded protein were found not to be triggered by urea, but instead, stabilized. The underlying mechanism of this stabilization is a favorable interaction of urea with transiently exposed, less-polar residues and the protein backbone, thereby impeding back-reactions. Taken together, these results suggest that, quite generally, urea-induced protein unfolding proceeds primarily not by active attack. Rather, thermal fluctuations toward the unfolded state are stabilized and the hydrophobic collapse of partially unfolded proteins toward the native state is impeded. As a result, the equilibrium is shifted toward the unfolded state.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.