ReviewJournal of molecular biology2020
Water as a Good Solvent for Unfolded Proteins: Folding and Collapse are Fundamentally Different.
Review in Journal of molecular biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
What it found
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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
25 citing papers in PubMed.
- New perspectives on plant water sensing.Science China. Life sciences · 2026Article
- pH-Dependent Stability and Cooperativity of Protein Unfolding from Differential Scanning Calorimetry Using FitFoldData.Biomolecules · 2026Article
- Article
- Accurate protein stability prediction for small domains using mega-scale experiments.bioRxiv : the preprint server for biology · 2026Article
- Cell-Free-Based Thermophilic Biocatalyst for the Synthesis of Amino Acids from One-Carbon Feedstocks.ACS synthetic biology · 2025Article
- Protein folding: basic statistical physics models and computational multipopulation genetic algorithms.Biophysical reviews · 2025Review
- Ionic liquids as stabilisers of therapeutic protein formulations: a review of insulin and monoclonal antibodies.Biophysical reviews · 2025Review
- The strand exchange domain of tumor suppressor PALB2 is intrinsically disordered and promotes oligomerization-dependent DNA compaction.iScience · 2024Article
- Stabilization of Non-Native Folds and Programmable Protein Gelation in Compositionally Designed Deep Eutectic Solvents.ACS nano · 2024Article
- The strand exchange domain of tumor suppressor PALB2 is intrinsically disordered and promotes oligomerization-dependent DNA compaction.bioRxiv : the preprint server for biology · 2024Article
- AutoRNC: An automated modeling program for building atomic models of ribosome-nascent chain complexes.Structure (London, England : 1993) · 2024Article
- The molecular basis for cellular function of intrinsically disordered protein regions.Nature reviews. Molecular cell biology · 2024Review
- Directing oat groat heat treatment conditions towards increased protein extractability.Current research in food science · 2024Article
- Sequence-ensemble-function relationships for disordered proteins in live cells.bioRxiv : the preprint server for biology · 2023Article
- Sequence-ensemble-function relationships for disordered proteins in live cells.Research square · 2023Article
- Cysteine Redox Chemistry in Peptide Self-Assembly to Modulate Hydrogelation.Molecules (Basel, Switzerland) · 2023Article
- The Action of Chemical Denaturants: From Globular to Intrinsically Disordered Proteins.Biology · 2023Review
- Getting Smaller by Denaturation: Acid-Induced Compaction of Antibodies.The journal of physical chemistry letters · 2023Article
- Deep mining of the protein energy landscape.Structural dynamics (Melville, N.Y.) · 2023Article
- Denatured State Conformational Biases in Three-Helix Bundles Containing Divergent Sequences Localize near Turns and Helix Capping Residues.Biochemistry · 2021Article
Corrections and comments
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Authors and funding
3 authors.
Funding
Abstract
The argument that the hydrophobic effect is the primary effect driving the folding of globular proteins is nearly universally accepted (including by the authors). But does this view also imply that water is a "poor" solvent for the unfolded states of these same proteins? Here we argue that the answer is "no," that is, folding to a well-packed, extensively hydrogen-bonded native structure differs fundamentally from the nonspecific chain collapse that defines a poor solvent. Thus, the observation that a protein folds in water does not necessitate that water is a poor solvent for its unfolded state. Indeed, chain-solvent interactions that are marginally more favorable than nonspecific intrachain interactions are beneficial to protein function because they destabilize deleterious misfolded conformations and inter-chain interactions.
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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.