ArticleBiophysical journal2021
Proteins maintain hydration at high [KCl] concentration regardless of content in acidic amino acids.
Article in Biophysical journal, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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7 citing papers in PubMed, 16 citations in OpenAlex.
- Functional characteristics and distribution of microorganisms in saline and alkaline soils and their probiotic effects: a review.Microbial cell factories · 2026Review
- Reduction of oxidative rancidification of fungal melanin-coated films in pork lard preservation in trading.International microbiology : the official journal of the Spanish Society for Microbiology · 2025Article
- How sensitive are protein hydration shells to electrolyte concentration and protein composition?Protein science : a publication of the Protein Society · 2025Article
- Ion-combination specific effects driving the enzymatic activity of halophilic alcohol dehydrogenase 2 fromRSC sustainability · 2024Article
- Electrostatics introduce a trade-off between mesophilic stability and adaptation in halophilic proteins.Protein science : a publication of the Protein Society · 2024Article
- Living in trinity of extremes: Genomic and proteomic signatures of halophilic, thermophilic, and pH adaptation.Current research in structural biology · 2024Article
- Prevalence and mechanism of synergistic carboxylate-cation-water interactions in halophilic proteins.Biophysical journal · 2023Article
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2 authors at 1 institution in 1 country.
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Abstract
Proteins of halophilic organisms, which accumulate molar concentrations of KCl in their cytoplasm, have a much higher content in acidic amino acids than proteins of mesophilic organisms. It has been proposed that this excess is necessary to maintain proteins hydrated in an environment with low water activity, either via direct interactions between water and the carboxylate groups of acidic amino acids or via cooperative interactions between acidic amino acids and hydrated cations. Our simulation study of five halophilic proteins and five mesophilic counterparts does not support either possibility. The simulations use the AMBER ff14SB force field with newly optimized Lennard-Jones parameters for the interactions between carboxylate groups and potassium ions. We find that proteins with a larger fraction of acidic amino acids indeed have higher hydration levels, as measured by the concentration of water in their hydration shell and the number of water/protein hydrogen bonds. However, the hydration level of each protein is identical at low (b
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