ArticleProtein science : a publication of the Protein Society2013
Thermal stability of lysozyme as a function of ion concentration: a reappraisal of the relationship between the Hofmeister series and protein stability.
Article in Protein science : a publication of the Protein Society, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
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Who cites it
33 citing papers in PubMed, 109 citations in OpenAlex.
- In vitro Sorption of Lysozyme in Reusable Silicone Hydrogel Contact Lenses: The Impact of Material and Care Solution.Clinical optometry · 2026Article
- Effect of Salts on the Aggregation and Strength of Protein-Based Underwater Adhesives.ACS omega · 2025Article
- Measuring the Thermal Unfolding of Lysozyme: A Critical Comparison of Differential Scanning Fluorimetry and Differential Scanning Calorimetry.ChemistryOpen · 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
- Hybrid Mass Spectrometry Applied across the Production of Antibody Biotherapeutics.Journal of the American Society for Mass Spectrometry · 2025Article
- Polymers for Disrupting Protein-Protein Interactions: Where Are We and Where Should We Be?Biomacromolecules · 2024Review
- CoVAMPnet: Comparative Markov State Analysis for Studying Effects of Drug Candidates on Disordered Biomolecules.JACS Au · 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
- Protein Dielectrophoresis with Gradient Array of Conductive Electrodes Sheds New Light on Empirical Theory.Analytical chemistry · 2023Article
- Effect of 1-Ethyl-3-methylimidazolium Tetrafluoroborate and Acetate Ionic Liquids on Stability and Amyloid Aggregation of Lysozyme.International journal of molecular sciences · 2022Article
- Weakly hydrated anions bind to polymers but not monomers in aqueous solutions.Nature chemistry · 2022Article
- The Effects of Temperature and Pressure on Protein-Ligand Binding in the Presence of Mars-Relevant Salts.Biology · 2021Article
- Electrostatic interaction optimization improves catalytic rates and thermotolerance on xylanases.Biophysical journal · 2021Article
- The high stability of the three-helix bundle UBA domain of p62 protein as revealed by molecular dynamics simulations.Journal of molecular modeling · 2021Article
- Cholesteryl-Conjugated Ribonuclease A Exhibits Enzyme Activity in Aqueous Solution and Resistance to Dimethyl Sulfoxide.ACS omega · 2021Article
- Preformulation Characterization and the Effect of Ionic Excipients on the Stability of a Novel DB Fusion Protein.Journal of pharmaceutical sciences · 2021Article
- Anion binding to ubiquitin and its relevance to the Hofmeister effects.Chemical science · 2020Article
- High pressures increase α-chymotrypsin enzyme activity under perchlorate stress.Communications biology · 2020Article
- Synthesis and Characterization of Cholesteryl Conjugated Lysozyme (CHLysozyme).Molecules (Basel, Switzerland) · 2020Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Anion and cation effects on the structural stability of lysozyme were investigated using differential scanning calorimetry. At low concentrations (<5 mM) anions and cations alter the stability of lysozyme but they do not follow the Hofmeister (or inverse Hofmeister) series. At higher concentrations protein stabilization follows the well-established Hofmeister series. Our hypothesis is that there are three mechanisms at work. At low concentrations the anions interact with charged side chains where the presence of the ion can alter the structural stability of the protein. At higher concentrations the low charge density anions perchlorate and iodide interact weakly with the protein. Their presence however reduces the Gibbs free energy required to hydrate the core of the protein that is exposed during unfolding therefore destabilizing the structure. At higher concentrations the high charge density anions phosphate and sulfate compete for water with the protein as it unfolds increasing the Gibbs free energy required to hydrate the newly exposed core of the protein therefore stabilizing the structure.
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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.