ArticleProceedings of the National Academy of Sciences of the United States of America1991
Binary-liquid phase separation of lens protein solutions.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1991. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 77 papers.
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Who cites it
77 citing papers in PubMed.
- Modeling Opposite Effects of an Additive on Liquid-Liquid Phase Separation and Crystal Solubility of Protein Solutions.Molecules (Basel, Switzerland) · 2026Article
- A label-free method for measuring the composition of multicomponent biomolecular condensates.Nature chemistry · 2025Article
- Yield of Protein Crystallization from Metastable Liquid-Liquid Phase Separation.Molecules (Basel, Switzerland) · 2025Article
- Transcription regulation by biomolecular condensates.Nature reviews. Molecular cell biology · 2025Review
- In the Beginning: Let Hydration Be Coded in Proteins for Manifestation and Modulation by Salts and Adenosine Triphosphate.International journal of molecular sciences · 2024Review
- A dual growth mode unique for organic crystals relies on mesoscopic liquid precursors.Communications chemistry · 2024Article
- Fundamental Aspects of Phase-Separated Biomolecular Condensates.Chemical reviews · 2024Review
- Testing mixing rules for structural and dynamical quantities in multi-component crowded protein solutions.APL bioengineering · 2024Article
- Diffusiophoresis of Macromolecules within the Framework of Multicomponent Diffusion.Molecules (Basel, Switzerland) · 2024Review
- Surface Charge Can Modulate Phase Separation of Multidomain Proteins.Journal of the American Chemical Society · 2024Article
- Protein Association in Solution: Statistical Mechanical Modeling.Biomolecules · 2023Review
- The mechanism of self-association of humanJournal of molecular liquids · 2023Article
- Article
- Atomistic modeling of liquid-liquid phase equilibrium explains dependence of critical temperature on γ-crystallin sequence.Communications biology · 2023Article
- Protein nanocondensates: the next frontier.Biophysical reviews · 2023Review
- Biomolecular phase separation in stress granule assembly and virus infection.Acta biochimica et biophysica Sinica · 2023Article
- Identification of Phase-Separation-Protein-Related Function Based on Gene Ontology by Using Machine Learning Methods.Life (Basel, Switzerland) · 2023Article
- Atomistic Modeling of Liquid-Liquid Phase Equilibrium Explains Dependence of Critical Temperature on γ-Crystallin Sequence.bioRxiv : the preprint server for biology · 2023Article
- 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
- Conformational Changes and Drivers of Monoclonal Antibody Liquid-Liquid Phase Separation.Journal of pharmaceutical sciences · 2023Article
17 more citing papers are in PubMed but not listed here.
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5 authors.
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Abstract
We have determined the coexistence curves (plots of phase-separation temperature T versus protein concentration C) for aqueous solutions of purified calf lens proteins. The proteins studied, calf gamma IIIa-, gamma IIIb-, and gamma IVa-crystallin, have very similar amino acid sequences and three-dimensional structures. Both ascending and descending limbs of the coexistence curves were measured. We find that the coexistence curves for each of these proteins and for gamma II-crystallin can be fit, near the critical point, to the function /(Cc-C)/Cc/ = A [(Tc - T)/Tc]beta, where beta = 0.325, Cc is the critical protein concentration in mg/ml, Tc is the critical temperature for phase separation in K, and A is a parameter that characterizes the width of the coexistence curve. We find that A and Cc are approximately the same for all four coexistence curves (A = 2.6 +/- 0.1, Cc = 289 +/- 20 mg/ml), but that Tc is not the same. For gamma II- and gamma IIIb-crystallin, Tc approximately 5 degrees C, whereas for gamma IIIa- and gamma IVa-crystallin, Tc approximately 38 degrees C. By comparing the published protein sequences for calf, rat, and human gamma-crystallins, we postulate that a few key amino acid residues account for the division of gamma-crystallins into low-Tc and high-Tc groups.
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