ArticleBiophysical journal2018
Ion Specificity and Nonmonotonic Protein Solubility from Salt Entropy.
Article in Biophysical journal, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed.
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- Binary Pea Protein-Psyllium Hydrogel: Insights into the Influence of pH and Ionic Strength on the Physical Stability and Mechanical Characteristics.Gels (Basel, Switzerland) · 2024Article
- Combined Effects of Pressure and Ionic Strength on Protein-Protein Interactions: An Empirical Approach.Biomacromolecules · 2024Article
- Prediction of Antibody Viscosity from Dilute Solution Measurements.Antibodies (Basel, Switzerland) · 2023Article
- Characterization ofMicrobiology spectrum · 2022Article
- High-level transient production of a protease-resistant mutant form of human basic fibroblast growth factor inPlant biotechnology (Tokyo, Japan) · 2022Article
- Deciphering how naturally occurring sequence features impact the phase behaviours of disordered prion-like domains.Nature chemistry · 2022Article
- How Hierarchical Interactions Make Membraneless Organelles Tick Like Clockwork.Trends in biochemical sciences · 2021Review
- Interplay of folded domains and the disordered low-complexity domain in mediating hnRNPA1 phase separation.Nucleic acids research · 2021Article
- Reentrant liquid condensate phase of proteins is stabilized by hydrophobic and non-ionic interactions.Nature communications · 2021Article
- Enhanced Solubility of Rapeseed Meal Protein Isolates Prepared by Sequential Isoelectric Precipitation.Foods (Basel, Switzerland) · 2020Article
- Polymer effects modulate binding affinities in disordered proteins.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Effects of non-pairwise repulsion on nanoparticle assembly.The Journal of chemical physics · 2019Article
- SLTCAP: A Simple Method for Calculating the Number of Ions Needed for MD Simulation.Journal of chemical theory and computation · 2018Article
Corrections and comments
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Authors and funding
2 authors.
Funding
Abstract
The addition of salt to protein solutions can either increase or decrease the protein solubility, and the magnitude of this effect depends on the salt used. We show that these effects can be captured using a theory that includes attractive and repulsive electrostatic interactions, nonelectrostatic protein-ion interactions, and ion-solvent interactions via an effective solvated ion radius. We find that the ion radius has significant effects on the translational entropy of the salt, which leads to salt specificity in the protein solubility. At low salt, the dominant effect comes from the entropic cost of confining ions within the aggregate, whereas at high concentrations, the salt drives a depletion attraction that favors aggregation. Our theory explains the reversal in the Hofmeister series observed in lysozyme cloud point measurements and semi-quantitatively describes the solubility of lysozyme and chymosin crystals. We present a comparison of the contributions to the free energy and give guidelines for when salting in or salting out should be expected.
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