ArticleRSC advances2019
Do soft anions promote protein denaturation through binding interactions? A case study using ribonuclease A.
Article in RSC advances, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 17 citations in OpenAlex.
- Biophysical characterization of Eag chaperones suggests the mechanism of effector transmembrane domain release.Nature communications · 2026Article
- Measuring the Thermal Unfolding of Lysozyme: A Critical Comparison of Differential Scanning Fluorimetry and Differential Scanning Calorimetry.ChemistryOpen · 2025Article
- The Streptococcus phage protein paratox is an intrinsically disordered protein.Protein science : a publication of the Protein Society · 2024Article
- Effectiveness of TRIzol in Inactivating Animal Pathogens.Applied biosafety : journal of the American Biological Safety Association · 2023Review
- Denaturation of proteins: electrostatic effectsRSC advances · 2022Article
- Perchlorate salts confer psychrophilic characteristics in α-chymotrypsin.Scientific reports · 2021Article
- Anion binding to ubiquitin and its relevance to the Hofmeister effects.Chemical science · 2020Article
- Adding Insult to Injury: Mechanistic Basis for How AmpC Mutations Allow Pseudomonas aeruginosa To Accelerate Cephalosporin Hydrolysis and Evade Avibactam.Antimicrobial agents and chemotherapy · 2020Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
It has long been known that large soft anions like bromide, iodide and thiocyanate are protein denaturing agents, but their mechanism of action is still unclear. In this work we have investigated the protein denaturing properties of these anions using Ribonuclease A (RNase A) as a model protein system. Salt-induced perturbations to the protein folding free energy were determined using differential scanning calorimetry and the results demonstrate that the addition of sodium iodide and sodium thiocyanate significantly decreases the melting temperature of the protein. In order to account for this reduction in protein stability, we show that the introduction of salts that contain soft anions to the aqueous solvent perturbs the protein unfolding free energy through three mechanisms: (a) screening Coulomb interactions that exist between charged protein residues, (b) Hofmeister effects, and (c) specific anion binding to CH and CH
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Registered trials
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