ArticleJournal of molecular modeling2016
Protein remains stable at unusually high temperatures when solvated in aqueous mixtures of amino acid based ionic liquids.
Article in Journal of molecular modeling, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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Who cites it
3 citing papers in PubMed, 16 citations in OpenAlex.
- Design of ionic liquids containing glucose and choline as drug carriers, finding the link between QM and MD studies.Scientific reports · 2022Article
- Insights into the Structure and Dynamics of Imidazolium Ionic Liquid and Tetraethylene Glycol Dimethyl Ether Cosolvent Mixtures: A Molecular Dynamics Approach.Nanomaterials (Basel, Switzerland) · 2021Article
- Aqueous ionic liquids in comparison with standard co-solutes : Differences and common principles in their interaction with protein and DNA structures.Biophysical reviews · 2018Review
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Authors and funding
3 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Using molecular dynamics simulations, we investigated the thermal stability and real-time denaturation of a model mini-protein in four solvents: (1) water, (2) 1-ethyl-3-methylimidazolium alaninate [EMIM][ALA] (5 mol% in water), (3) methioninate [EMIM][MET] (5 mol% in water), and (4) tryptophanate [EMIM][TRP] (5 mol% in water). Upon analyzing the radius of gyration, the solvent-accessible surface area, root-mean-squared deviations, and inter- and intramolecular hydrogen bonds, we found that the mini-protein remains stable at 30-40 K higher temperatures in aqueous amino acid based ionic liquids (AAILs) than in water. This thermal stability was correlated with the thermodynamics and shear viscosity of the AAIL-containing mixtures. These results suggest that AAILs are generally favorable for protein conservation. Graphical Abstract Conformation of the [TRP]-cage mini-protein in an aqueous amino acid based ionic liquid (AAIL).
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