ArticleCommunications chemistry2024
Interactions between the protein barnase and co-solutes studied by NMR.
Article in Communications chemistry, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 12 citations in OpenAlex.
- Mimetics of in-cell and subcellular crowding and solvation for protein folding.Biochemical Society transactions · 2026Review
- Superchaotropic Stabilization of Monomeric Protein States.Biomacromolecules · 2026Article
- Improvement in protein HSQC spectra from addition of betaine.Journal of biomolecular NMR · 2025Article
- Selective Ion Binding and Uptake Shape the Microenvironment of Biomolecular Condensates.Journal of the American Chemical Society · 2025Article
- Weak, specific chemical interactions dictate barnase stability in diverse cellular environments.Protein science : a publication of the Protein Society · 2025Article
- Anion-Facilitated Hydrogen-Deuterium Exchange as a Tool to Probe Weak Anion-Protein Interactions Responsible for Hofmeister Effects.The journal of physical chemistry. B · 2025Article
- Characterizing Interactions Between Small Peptides and Dimethyl Sulfoxide Using Infrared Spectroscopy and Computational Methods.Molecules (Basel, Switzerland) · 2024Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Protein solubility and stability depend on the co-solutes present. There is little theoretical basis for selection of suitable co-solutes. Some guidance is provided by the Hofmeister series, an empirical ordering of anions according to their effect on solubility and stability; and by osmolytes, which are small organic molecules produced by cells to allow them to function in stressful environments. Here, NMR titrations of the protein barnase with Hofmeister anions and osmolytes are used to measure and locate binding, and thus to separate binding and bulk solvent effects. We describe a rationalisation of Hofmeister (and inverse Hofmeister) effects, which is similar to the traditional chaotrope/kosmotrope idea but based on solvent fluctuation rather than water withdrawal, and characterise how co-solutes affect protein stability and solubility, based on solvent fluctuations. This provides a coherent explanation for solute effects, and points towards a more rational basis for choice of excipients.
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What OpenQuestion holds
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.