ArticleScientific reports2016
The effects of organic solvents on the folding pathway and associated thermodynamics of proteins: a microscopic view.
Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 62 citations in OpenAlex.
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- A Computational Perspective to Intermolecular Interactions and the Role of the Solvent on Regulating Protein Properties.Chemical reviews · 2025Review
- Protein codes promote selective subcellular compartmentalization.Science (New York, N.Y.) · 2025Article
- Assembly of oleosin during efficient extraction: Altering the sequence of defatting solvents.Food chemistry: X · 2025Article
- Protein codes promote selective subcellular compartmentalization.bioRxiv : the preprint server for biology · 2024Article
- Review
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- Can we achieve biomimetic electrospun scaffolds with gelatin alone?Frontiers in bioengineering and biotechnology · 2023Article
- Role of ionic liquids on stabilization of therapeutic proteins and model proteins.The protein journal · 2022Review
- A Conformationally Stable Acyclic β-Hairpin Scaffold Tolerating the Incorporation of Poorly β-Sheet-Prone Amino Acids.Chembiochem : a European journal of chemical biology · 2022Article
- Antiviral activities of natural compounds and ionic liquids to inhibit the Mpro of SARS-CoV-2: a computational approach.RSC advances · 2022Article
- Diamine Oxidase-Conjugated Multiwalled Carbon Nanotubes to Facilitate Electrode Surface Homogeneity.Sensors (Basel, Switzerland) · 2022Article
- Solubilization and Refolding of Inclusion Body Proteins.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Removal of Persistent Sulfamethoxazole and Carbamazepine from Water by Horseradish Peroxidase Encapsulated into Poly(Vinyl Chloride) Electrospun Fibers.International journal of molecular sciences · 2021Article
- An investigation of alkaline phosphatase enzymatic activity after electrospinning and electrospraying.Journal of drug delivery science and technology · 2021Article
- Water-Soluble Iridium Photoredox Catalyst for the Trifluoromethylation of Biomolecule Substrates in Phosphate Buffered Saline Solvent.Organic letters · 2021Article
- Development of a Fast Organic Extraction-Precipitation Method for Improved Purification of Elastin-Like Polypeptides That Is Independent of Sequence and Molecular Weight.Biomacromolecules · 2021Article
- Increasing Solvent Tolerance to Improve Microbial Production of Alcohols, Terpenoids and Aromatics.Microorganisms · 2021Review
- Protein Stability in Titan's Subsurface Water Ocean.Astrobiology · 2020Article
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Protein folding is subject to the effects of solvation environment. A variety of organic solvents are used as additives for in vitro refolding of denatured proteins. Examination of the solvent effects on protein folding could be of fundamental importance to understand the molecular interactions in determining protein structure. This article investigated the folding of α-helix and β-hairpin structures in water and the solutions of two representative refolding additives (methanol (MeOH) and 1-Ethyl-3-methylimidazolium chloride (EMIM-Cl) ionic liquid) using REMD simulations. For both α-helix and β-hairpin in MeOH/water solution or α-helix in EMIM-Cl/water solution, the transient structures along the folding pathway are consistent with the counterparts in water but the relative statistical weights are changed, leading to the decrease in the overall folding free energy barrier. Accordingly, MeOH promotes the folding of both α-helix and β-hairpin but EMIM-Cl ionic liquid only promotes the folding of α-helix, consistent with experimental observations. The present study reveals for the first time the trivial effects on folding route but significant effects on folding thermodynamics from MeOH and EMIM-Cl, explaining the function of protein refolding additives and testifying the validity of the folding mechanism revealed by in vitro protein folding study using refolding additives.
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