ArticleBiophysical journal2012
Anisotropy of the Coulomb interaction between folded proteins: consequences for mesoscopic aggregation of lysozyme.
Article in Biophysical journal, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed.
- A nonclassical pathway of β-hematin crystal nucleation enables its suppression by antimalarials.Communications chemistry · 2025Article
- Mesoscopic p53-rich clusters represent a new class of protein condensates.Biophysics reviews · 2025Review
- A dual growth mode unique for organic crystals relies on mesoscopic liquid precursors.Communications chemistry · 2024Article
- 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
- The Role of Surface Exposed Lysine in Conformational Stability and Functional Properties of Lipase fromMolecules (Basel, Switzerland) · 2020Article
- A mechanism for reversible mesoscopic aggregation in liquid solutions.Nature communications · 2019Article
- Anomalous Dense Liquid Condensates Host the Nucleation of Tumor Suppressor p53 Fibrils.iScience · 2019Article
- Model for screened, charge-regulated electrostatics of an eye lens protein: Bovine gammaB-crystallin.Physical review. E · 2017Article
- Lack of Dependence of the Sizes of the Mesoscopic Protein Clusters on Electrostatics.Biophysical journal · 2015Article
- Nucleation precursors in protein crystallization.Acta crystallographica. Section F, Structural biology communications · 2014Review
- On the characterization of intermediates in the isodesmic aggregation pathway of hen lysozyme at alkaline pH.PloS one · 2014Article
Corrections and comments
- Erratum issued
Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Toward quantitative description of protein aggregation, we develop a computationally efficient method to evaluate the potential of mean force between two folded protein molecules that allows for complete sampling of their mutual orientation. Our model is valid at moderate ionic strengths and accounts for the actual charge distribution on the surface of the molecules, the dielectric discontinuity at the protein-solvent interface, and the possibility of protonation or deprotonation of surface residues induced by the electric field due to the other protein molecule. We apply the model to the protein lysozyme, whose solutions exhibit both mesoscopic clusters of protein-rich liquid and liquid-liquid separation; the former requires that protein form complexes with typical lifetimes of approximately milliseconds. We find the electrostatic repulsion is typically lower than the prediction of the Derjaguin-Landau-Verwey-Overbeek theory. The Coulomb interaction in the lowest-energy docking configuration is nonrepulsive, despite the high positive charge on the molecules. Typical docking configurations barely involve protonation or deprotonation of surface residues. The obtained potential of mean force between folded lysozyme molecules is consistent with the location of the liquid-liquid coexistence, but produces dimers that are too short-lived for clusters to exist, suggesting lysozyme undergoes conformational changes during cluster formation.
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