ReviewPhilosophical transactions of the Royal Society of London. Series B, Biological sciences2004
Protein structure, stability and solubility in water and other solvents.
Review in Philosophical transactions of the Royal Society of London. Series B, Biological sciences, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 96 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
96 citing papers in PubMed, 381 citations in OpenAlex.
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- Quantitative Analysis of Amyloid Fibril Nucleation by Linking Folding and Nucleation Pathways Using a Robust Ultrasonic Assay.ACS omega · 2026Article
- Assessment of Marine Microalgae's Bioactive Extracts Potential for Food Applications.Molecular nutrition & food research · 2026Article
- Fibrin Glues: Proteins, Mechanism of Action, Classification, and Application.International journal of molecular sciences · 2025Review
- Stabilising proteins in solution using affordable and readily available small molecules.Biophysical reviews · 2025Review
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- Innovative Formulation Platform: Paving the Way for Superior Protein Therapeutics with Enhanced Efficacy and Broadened Applications.Advanced materials (Deerfield Beach, Fla.) · 2024Review
- Martini 3 OliGo̅mers: A Scalable Approach for Multimers and Fibrils in GROMACS.Journal of chemical theory and computation · 2024Article
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- Solvent constraints for biopolymer folding and evolution in extraterrestrial environments.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Protecting Proteins from Desiccation Stress Using Molecular Glasses and Gels.Chemical reviews · 2024Review
- Do Ionic Liquids Exhibit the Required Characteristics to Dissolve, Extract, Stabilize, and Purify Proteins? Past-Present-Future Assessment.Chemical reviews · 2024Review
- Systematic enhancement of protein crystallization efficiency by bulk lysine-to-arginine (KR) substitution.Protein science : a publication of the Protein Society · 2024Article
- Convergent behavior of extended stalk regions from staphylococcal surface proteins with widely divergent sequence patterns.Protein science : a publication of the Protein Society · 2023Article
- Combination of Milk and Plant Proteins to Develop Novel Food Systems: What Are the Limits?Foods (Basel, Switzerland) · 2023Review
- Intraspecific Variability in Proteomic Profiles and Biological Activities of the Honey Bee Hemolymph.Insects · 2023Article
- Extraction of Mycosporine-like Amino Acids and Proteins from the AgarophyteFoods (Basel, Switzerland) · 2023Article
36 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Proteins carry out the most difficult tasks in living cells. They do so by interacting specifically with other molecules. This requires that they fold to a unique, globular conformation that is only marginally more stable than the large ensemble of unfolded states. The folded state is stabilized mainly by the burial and tight packing of over 80% of the peptide groups and non-polar side chains. If life as we know it is to exist in a solvent other than water, the folded state must be stable and soluble in the new solvent. Our analysis suggests that proteins will be unstable in most polar solvents such as ethanol, extremely stable in non-polar solvents such as cyclohexane, and even more stable in a vacuum. Our solubility studies suggest that protein solubility will be markedly lower in polar solvents such as ethanol and that proteins will be essentially insoluble in non-polar solvents such as cyclohexane. For these and other reasons it seems unlikely that the life we know could exist in any solvent system other than water.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.