ArticleProceedings of the National Academy of Sciences of the United States of America2009
Urea, but not guanidinium, destabilizes proteins by forming hydrogen bonds to the peptide group.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 113 papers.
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Who cites it
113 citing papers in PubMed, 388 citations in OpenAlex.
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- Effects of Charge Sequence Pattern and Lysine-to-Arginine Substitution on the Structural Stability of Bioinspired Polyampholytes.Biomacromolecules · 2024Article
- Denaturing mass photometry for rapid optimization of chemical protein-protein cross-linking reactions.Nature communications · 2024Article
- Systematic enhancement of protein crystallization efficiency by bulk lysine-to-arginine (KR) substitution.Protein science : a publication of the Protein Society · 2024Article
- Folding of prestin's anion-binding site and the mechanism of outer hair cell electromotility.eLife · 2023Article
- Design, structure and plasma binding of ancestral β-CoV scaffold antigens.Nature communications · 2023Article
- Molecular mechanism of the common and opposing cosolvent effects of fluorinated alcohol and urea on a coiled coil protein.Protein science : a publication of the Protein Society · 2023Article
- Stabilizing α-Helicity of a Polypeptide in Aqueous Urea: Dipole Orientation or Hydrogen Bonding?ACS macro letters · 2023Article
- Myosin light chain of shark fast skeletal muscle exhibits intrinsic urea-resistibility.Scientific reports · 2023Article
- Guanidinium and amide CEST mapping of human brain by high spectral resolution CEST at 3 T.Magnetic resonance in medicine · 2023Article
53 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 3 institutions in 2 countries.
Funding
Abstract
The mechanism by which urea and guanidinium destabilize protein structure is controversial. We tested the possibility that these denaturants form hydrogen bonds with peptide groups by measuring their ability to block acid- and base-catalyzed peptide hydrogen exchange. The peptide hydrogen bonding found appears sufficient to explain the thermodynamic denaturing effect of urea. Results for guanidinium, however, are contrary to the expectation that it might H-bond. Evidently, urea and guanidinium, although structurally similar, denature proteins by different mechanisms.
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Registered trials
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.