ArticleThe journal of physical chemistry. B2012
Solute's perspective on how trimethylamine oxide, urea, and guanidine hydrochloride affect water's hydrogen bonding ability.
Article in The journal of physical chemistry. B, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
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Who cites it
11 citing papers in PubMed.
- Hydration of Simple Model Peptides in Aqueous Osmolyte Solutions.International journal of molecular sciences · 2021Article
- Effect of Osmolytes on Conformational Behavior of Intrinsically Disordered Protein α-Synuclein.Biophysical journal · 2019Article
- TrimethylamineProceedings of the National Academy of Sciences of the United States of America · 2017Article
- Do guanidinium and tetrapropylammonium ions specifically interact with aromatic amino acid side chains?Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Infrared and Fluorescence Assessment of Protein Dynamics: From Folding to Function.The journal of physical chemistry. B · 2016Article
- Site-specific infrared probes of proteins.Annual review of physical chemistry · 2015Review
- Regulation and aggregation of intrinsically disordered peptides.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- 2D IR spectroscopy of histidine: probing side-chain structure and dynamics via backbone amide vibrations.The journal of physical chemistry. B · 2014Article
- Microscopic insights into the protein-stabilizing effect of trimethylamine N-oxide (TMAO).Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Structure and dynamics of urea/water mixtures investigated by vibrational spectroscopy and molecular dynamics simulation.The journal of physical chemistry. B · 2013Article
- Protein Denaturation with Guanidinium: A 2D-IR Study.The journal of physical chemistry letters · 2013Article
Corrections and comments
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Authors and funding
2 authors.
Funding
Abstract
While the thermodynamic effects of trimethylamine oxide (TMAO), urea, and guanidine hydrochloride (GdnHCl) on protein stability are well understood, the underlying mechanisms of action are less well characterized and, in some cases, even under debate. Herein, we employ the stretching vibration of two infrared (IR) reporters, i.e., nitrile (C≡N) and carbonyl (C═O), to directly probe how these cosolvents mediate the ability of water to form hydrogen bonds with the solute of interest, e.g., a peptide. Our results show that these three agents, despite having different effects on protein stability, all act to decrease the strength of the hydrogen bonds formed between water and the infrared probe. While the behavior of TMAO appears to be consistent with its protein-protecting ability, those of urea and GdnHCl are inconsistent with their role as protein denaturants. The latter is of particular interest as it provides strong evidence indicating that although urea and GdnHCl can perturb the hydrogen-bonding property of water their protein-denaturing ability does not arise from a simple indirect mechanism.
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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.