ArticleProceedings of the National Academy of Sciences of the United States of America2011
Quantifying why urea is a protein denaturant, whereas glycine betaine is a protein stabilizer.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 72 papers.
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Who cites it
72 citing papers in PubMed, 229 citations in OpenAlex.
- Too close for comfort: Self-crowding transforms protein structure and stability beyond volume exclusion.Protein science : a publication of the Protein Society · 2026Article
- Effects of Loop Nucleobase Substitution on G-Quadruplex Thermal Stability in Aqueous Glycine Betaine, Proline, TMAO, and Urea Solutions.Biomolecules · 2026Article
- Changes in Water Dynamics by Osmolytes Regulate Enzyme Activity.The journal of physical chemistry. B · 2026Article
- Article
- Static and Dynamic Correlations in Binary and Ternary Mixtures of TMAO, Urea, and Water.The journal of physical chemistry. B · 2025Article
- Generation of shark single-domain antibodies as an aid for Cryo-EM structure determination of membrane proteins: Use hyaluronan synthase as an example.Journal of structural biology: X · 2025Article
- Crowding-induced stabilization and destabilization in a single protein.Protein science : a publication of the Protein Society · 2025Article
- Osmolyte-induced protein stability changes explained by graph theory.Computational and structural biotechnology journal · 2024Article
- Salt Effects on Caffeine across Concentration Regimes.The journal of physical chemistry. B · 2023Article
- Quantifying Amide-Aromatic Interactions at Molecular and Atomic Levels: Experimentally-determined Enthalpic and Entropic Contributions to Interactions of Amide spbioRxiv : the preprint server for biology · 2023Article
- Critical Beginnings: Selective Tuning of Solubility and Structural Accuracy of Newly Synthesized Proteins by the Hsp70 Chaperone System.The journal of physical chemistry. B · 2023Article
- Dehydration does not affect lipid-based hydration lubrication.Nanoscale · 2022Article
- Mechanism of Osmolyte Stabilization-Destabilization of Proteins: Experimental Evidence.The journal of physical chemistry. B · 2022Article
- Article
- Atomic view of cosolute-induced protein denaturation probed by NMR solvent paramagnetic relaxation enhancement.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Heterologous Production of Glycine Betaine UsingFrontiers in bioengineering and biotechnology · 2021Article
- Experimentally determined strengths of favorable and unfavorable interactions of amide atoms involved in protein self-assembly in water.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Conformational dynamics of superoxide dismutase (SOD1) in osmolytes: a molecular dynamics simulation study.RSC advances · 2020Article
- Quantitative Interpretation of Solvent Paramagnetic Relaxation for Probing Protein-Cosolute Interactions.Journal of the American Chemical Society · 2020Article
- Dynamical Model for the Counteracting Effects of TrimethylamineThe journal of physical chemistry. B · 2020Article
12 more citing papers are in PubMed but not listed here.
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
To explain the large, opposite effects of urea and glycine betaine (GB) on stability of folded proteins and protein complexes, we quantify and interpret preferential interactions of urea with 45 model compounds displaying protein functional groups and compare with a previous analysis of GB. This information is needed to use urea as a probe of coupled folding in protein processes and to tune molecular dynamics force fields. Preferential interactions between urea and model compounds relative to their interactions with water are determined by osmometry or solubility and dissected using a unique coarse-grained analysis to obtain interaction potentials quantifying the interaction of urea with each significant type of protein surface (aliphatic, aromatic hydrocarbon (C); polar and charged N and O). Microscopic local-bulk partition coefficients K(p) for the accumulation or exclusion of urea in the water of hydration of these surfaces relative to bulk water are obtained. K(p) values reveal that urea accumulates moderately at amide O and weakly at aliphatic C, whereas GB is excluded from both. These results provide both thermodynamic and molecular explanations for the opposite effects of urea and glycine betaine on protein stability, as well as deductions about strengths of amide NH--amide O and amide NH--amide N hydrogen bonds relative to hydrogen bonds to water. Interestingly, urea, like GB, is moderately accumulated at aromatic C surface. Urea m-values for protein folding and other protein processes are quantitatively interpreted and predicted using these urea interaction potentials or K(p) values.
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