ArticleJournal of the American Chemical Society2011
Anion binding to hydrophobic concavity is central to the salting-in effects of Hofmeister chaotropes.
Article in Journal of the American Chemical Society, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.
What it found
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Who cites it
53 citing papers in PubMed, 210 citations in OpenAlex.
- Experimental and theoretical investigation of zwitterionic surfactant adsorption on calcite for enhanced oil recovery.Scientific reports · 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
- Optimal Dielectric Boundary for Binding Free Energy Estimates in the Implicit Solvent.Journal of chemical information and modeling · 2024Article
- Determining Ion-Pair Binding Affinities of Heteroditopic Receptor Systems.Chemistry (Weinheim an der Bergstrasse, Germany) · 2024Article
- Complexity associated with caprylate binding to bovine serum albumin: Dimerization, allostery, and variance between the change in free energy and enthalpy of binding.Protein science : a publication of the Protein Society · 2024Article
- Greasy Cations Bind to Neutral Macromolecules in Aqueous Solution.The journal of physical chemistry letters · 2024Article
- Understanding the Phase Behavior of a Multistimuli-Responsive Elastin-like Polymer: Insights from Dynamic Light Scattering Analysis.The journal of physical chemistry. B · 2024Article
- Anion Binding to Ammonium and Guanidinium Hosts: Implications for the Reverse Hofmeister Effects Induced by Lysine and Arginine Residues.The Journal of organic chemistry · 2024Article
- Assessing Weak Anion Binding to Small Peptides.The journal of physical chemistry. B · 2024Article
- Solvent effects in anion recognition.Nature reviews. Chemistry · 2024Review
- Live-Cell Imaging to Resolve Salt-Induced Liquid-Liquid Phase Separation of FUS Protein by Dye Self-Labeling.Chemical & biomedical imaging · 2024Article
- Hofmeister Effects Shine in Nanoscience.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2023Review
- Accurate Host-Guest Binding Free Energies Using the AMOEBA Polarizable Force Field.Journal of chemical information and modeling · 2023Article
- An updated synthesis ofSupramolecular chemistry · 2023Article
- Anti-Hofmeister Anion Selectivity via a Mechanical Bond Effect in Neutral Halogen-Bonding [2]Rotaxanes.Angewandte Chemie (International ed. in English) · 2022Article
- An overview of the SAMPL8 host-guest binding challenge.Journal of computer-aided molecular design · 2022Article
- When Molecules Meet in Water-Recent Contributions of Supramolecular Chemistry to the Understanding of Molecular Recognition Processes in Water.ChemistryOpen · 2022Review
- Molecular Probes, Chemosensors, and Nanosensors for Optical Detection of Biorelevant Molecules and Ions in Aqueous Media and Biofluids.Chemical reviews · 2022Review
- Weakly hydrated anions bind to polymers but not monomers in aqueous solutions.Nature chemistry · 2022Article
- Coordination Cages Selectively Transport Molecular Cargoes Across Liquid Membranes.Journal of the American Chemical Society · 2021Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
For over 120 years it has been appreciated that certain salts (kosmotropes) cause the precipitation of proteins, while others (chaotropes) increase their solubility. The cause of this "Hofmeister effect" is still unclear, especially with the original concept that kosmotropic anions "make" water structure and chaotropes "break" it being countered by recent studies suggesting otherwise. Here, we present the first direct evidence that chaotropic anions have an affinity for hydrophobic concavity and that it is competition between a convex hydrophobe and the anion for a binding site that leads to the apparent weakening of the hydrophobic effect by chaotropes. In combination, these results suggest that chaotropes primarily induce protein solubilization by direct binding to concavity in the molten globule state of a protein.
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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.