ArticleSoft matter2016
Modeling phase transitions in mixtures of β-γ lens crystallins.
Article in Soft matter, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed.
- Protein Association in Solution: Statistical Mechanical Modeling.Biomolecules · 2023Review
- Engineering synthetic biomolecular condensates.Nature reviews bioengineering · 2023Review
- Numerical Techniques for Applications of Analytical Theories to Sequence-Dependent Phase Separations of Intrinsically Disordered Proteins.Methods in molecular biology (Clifton, N.J.) · 2023Article
- The influence of excipients on the viscosity of monoclonal antibody solutions.Journal of molecular liquids · 2022Article
- Phase stability of aqueous mixtures of bovine serum albumin with low molecular mass salts in presence of polyethylene glycol.Journal of molecular liquids · 2022Article
- Assembly of model postsynaptic densities involves interactions auxiliary to stoichiometric binding.Biophysical journal · 2022Article
- The Protein Folding Problem: The Role of Theory.Journal of molecular biology · 2021Review
- Liquid network connectivity regulates the stability and composition of biomolecular condensates with many components.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Biomolecular Chemistry in Liquid Phase Separated Compartments.Frontiers in molecular biosciences · 2019Review
- Modeling the depletion effect caused by an addition of polymer to monoclonal antibody solutions.Journal of physics. Condensed matter : an Institute of Physics journal · 2018Article
- Controlling the viscosities of antibody solutions through control of their binding sites.Journal of molecular liquids · 2018Article
- Theory for the Liquid-Liquid Phase Separation in Aqueous Antibody Solutions.The journal of physical chemistry. B · 2018Article
- Liquid-Liquid Phase Separation of Patchy Particles Illuminates Diverse Effects of Regulatory Components on Protein Droplet Formation.Scientific reports · 2018Article
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Authors and funding
3 authors.
Funding
Abstract
We analyze the experimentally determined phase diagram of a γD-βB1 crystallin mixture. Proteins are described as dumbbells decorated with attractive sites to allow inter-particle interaction. We use thermodynamic perturbation theory to calculate the free energy of such mixtures and, by applying equilibrium conditions, also the compositions and concentrations of the co-existing phases. Initially we fit the Tcloudversus packing fraction η measurements for a pure (x2 = 0) γD solution in 0.1 M phosphate buffer at pH = 7.0. Another piece of experimental data, used to fix the model parameters, is the isotherm x2vs. η at T = 268.5 K, at the same pH and salt content. We use the conventional Lorentz-Berthelot mixing rules to describe cross interactions. This enables us to determine: (i) model parameters for pure βB1 crystallin protein and to calculate; (ii) complete equilibrium surface (Tcloud-x2-η) for the crystallin mixtures. (iii) We present the results for several isotherms, including the tie-lines, as also the temperature-packing fraction curves. Good agreement with the available experimental data is obtained. An interesting result of these calculations is evidence of the coexistence of three phases. This domain appears for the region of temperatures just out of the experimental range studied so far. The input parameters, leading good description of experimental data, revealed a large difference between the numbers of the attractive sites for γD and βB1 proteins. This interesting result may be related to the fact that γD has a more than nine times smaller quadrupole moment than its partner in the mixture.
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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.