ArticleNature communications2019
A mechanism for reversible mesoscopic aggregation in liquid solutions.
Article in Nature communications, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed.
- Navigating Classical and Nonclassical Realms of Nucleation and Crystallization.Small (Weinheim an der Bergstrasse, Germany) · 2026Review
- Spectrin condensates provide a nidus for assembling the axonal membrane-associated periodic skeleton.iScience · 2026Article
- A nonclassical pathway of β-hematin crystal nucleation enables its suppression by antimalarials.Communications chemistry · 2025Article
- Tafenoquine Disrupts Intraerythrocytic Stages of Malaria Parasites by Inhibiting Nonclassical Pathways of β-Hematin Nucleation and Growth.Biochemistry · 2025Article
- Chemical reaction motifs driving non-equilibrium behaviours in phase separating materials.Journal of the Royal Society, Interface · 2023Article
- Intermolecular interactions underlie protein/peptide phase separation irrespective of sequence and structure at crowded milieu.Nature communications · 2023Article
- A workflow for the development of template-assisted membrane crystallization downstream processing for monoclonal antibody purification.Nature protocols · 2023Review
- Protein nanocondensates: the next frontier.Biophysical reviews · 2023Review
- Rational Design of a Self-Assembling High Performance Organic Nanofluorophore for Intraoperative NIR-II Image-Guided Tumor Resection of Oral Cancer.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2023Article
- Nucleation of glucose isomerase protein crystals in a nonclassical disguise: The role of crystalline precursors.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Protein conformation and biomolecular condensates.Current research in structural biology · 2022Review
- Mesoscopic protein-rich clusters host the nucleation of mutant p53 amyloid fibrils.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
Corrections and comments
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Authors and funding
2 authors.
Funding
Abstract
Solutions of proteins and other molecules exhibit puzzling, mesoscopically sized inclusions of a solute-rich liquid, well outside the region of stability of the solute-rich phase. This mesoscopic size is in conflict with existing views on heterophase fluctuations. Here we systematically work out a microscopic mechanism by which a metastable solute-rich phase can readily nucleate in a liquid solution. A requisite component of the mechanism is that the solute form long-lived complexes with itself or other molecules. After nucleated in this non-classical fashion, individual droplets grow until becoming mechanically unstable because of a concomitant drop in the internal pressure, the drop caused by the metastability of the solute-rich phase. The ensemble of the droplets is steady-state. In a freshly prepared solution, the ensemble is predicted to evolve in a way similar to the conventional Ostwald ripening, during which larger droplets grow at the expense of smaller droplets.
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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.