ArticleBiophysical journal2015
Lack of Dependence of the Sizes of the Mesoscopic Protein Clusters on Electrostatics.
Article in Biophysical journal, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed.
- 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
- Mesoscopic p53-rich clusters represent a new class of protein condensates.Biophysics reviews · 2025Review
- Protein aggregates and biomolecular condensates: implications for human health and disease.Frontiers in molecular biosciences · 2025Review
- A dual growth mode unique for organic crystals relies on mesoscopic liquid precursors.Communications chemistry · 2024Article
- Intermolecular interactions underlie protein/peptide phase separation irrespective of sequence and structure at crowded milieu.Nature communications · 2023Article
- 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
- Topological Considerations in Biomolecular Condensation.Biomolecules · 2023Review
- Phase-separating RNA-binding proteins form heterogeneous distributions of clusters in subsaturated solutions.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Article
- 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
- 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
- Article
- Whole-Cell Models and Simulations in Molecular Detail.Annual review of cell and developmental biology · 2019Review
- Anomalous Dense Liquid Condensates Host the Nucleation of Tumor Suppressor p53 Fibrils.iScience · 2019Article
- Dynamics of liquid-liquid phase separation of wheat gliadins.Scientific reports · 2018Article
- Tuning crystallization pathways through sequence engineering of biomimetic polymers.Nature materials · 2017Article
- Staying Together: Protein Molecules in Mesoscopic Clusters.Biophysical journal · 2015Article
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Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Protein-rich clusters of steady submicron size and narrow size distribution exist in protein solutions in apparent violation of the classical laws of phase equilibrium. Even though they contain a minor fraction of the total protein, evidence suggests that they may serve as essential precursors for the nucleation of ordered solids such as crystals, sickle-cell hemoglobin polymers, and amyloid fibrils. The cluster formation mechanism remains elusive. We use the highly basic protein lysozyme at nearly neutral and lower pH as a model and explore the response of the cluster population to the electrostatic forces, which govern numerous biophysical phenomena, including crystallization and fibrillization. We tune the strength of intermolecular electrostatic forces by varying the solution ionic strength I and pH and find that despite the weaker repulsion at higher I and pH, the cluster size remains constant. Cluster responses to the presence of urea and ethanol demonstrate that cluster formation is controlled by hydrophobic interactions between the peptide backbones, exposed to the solvent after partial protein unfolding that may lead to transient protein oligomers. These findings reveal that the mechanism of the mesoscopic clusters is fundamentally different from those underlying the two main classes of ordered protein solid phases, crystals and amyloid fibrils, and partial unfolding of the protein chain may play a significant role.
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