ArticlePhysical chemistry chemical physics : PCCP2018
Ion-specificity and surface water dynamics in protein solutions.
Article in Physical chemistry chemical physics : PCCP, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed.
- On the Local Structure of Water Surrounding Inorganic Anions Within Layered Double Hydroxides.Molecules (Basel, Switzerland) · 2025Article
- Dynamical Transition in Dehydrated Proteins.The journal of physical chemistry letters · 2024Article
- Do Ionic Liquids Exhibit the Required Characteristics to Dissolve, Extract, Stabilize, and Purify Proteins? Past-Present-Future Assessment.Chemical reviews · 2024Review
- Extraction of Polyphenols from Slovenian Hop (Plants (Basel, Switzerland) · 2023Article
- Decreased Water Mobility Contributes To Increased α-Synuclein Aggregation.Angewandte Chemie (Weinheim an der Bergstrasse, Germany) · 2023Article
- Decreased Water Mobility Contributes To Increased α-Synuclein Aggregation.Angewandte Chemie (International ed. in English) · 2023Article
- Ion influence on surface water dynamics and proton exchange at protein surfaces - A unified model for transverse and longitudinal NMR relaxation dispersion.Journal of molecular liquids · 2022Article
- Phase stability of aqueous mixtures of bovine serum albumin with low molecular mass salts in presence of polyethylene glycol.Journal of molecular liquids · 2022Article
- Effect of Buffer on Protein Stability in Aqueous Solutions: A Simple Protein Aggregation Model.The journal of physical chemistry. B · 2021Article
- Studying the mechanism of phase separation in aqueous solutions of globular proteinsPhysical chemistry chemical physics : PCCP · 2021Article
- Hofmeister Series: Insights of Ion Specificity from Amphiphilic Assembly and Interface Property.ACS omega · 2020Review
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Authors and funding
8 authors.
Funding
Abstract
Ion-specific effects at the protein surface are investigated here in light of the changes they infer to surface water dynamics, as observed by 1H NMR relaxation (at 20 MHz). Two well-known proteins, hen egg-white lysozyme (LZM) and bovine serum albumin (BSA), show qualitatively opposite trends in the transverse relaxation rate, R2(1H), along a series of different monovalent salt anions in the solution. Presence of salt ions increases R2(1H) in the case of lysozyme and diminishes it in the case of BSA. The effect magnifies for larger and more polarizable ions. The same contrasting effect between the two proteins is observed for protein-solvent proton exchange. This hints at subtle effects ion-binding might have on the accessibility of water surface sites on the protein. We suggest that the combination of the density of surface charge residues and surface roughness, at the atomic scale, dictates the response to the presence of salt ions and is proper to each protein. Further, a dramatic increase in R2(1H) is found to correlate closely with the formation of protein aggregates. The same ordering of salts in their ability to aggregate lysozyme, as seen previously by cloud point measurements, is reproduced here by R2(1H). 1H NMR relaxation data is supplemented by 35Cl and 14N NMR relaxation for selected salt ions to probe the ion-binding itself.
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