ArticleInternational journal of molecular sciences2021
Solubility and Aggregation of Selected Proteins Interpreted on the Basis of Hydrophobicity Distribution.
Article in International journal of molecular sciences, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed.
- Bridging Generative AI and Diffusion Models With Molecular Simulation to Design Anti-Quorum-Sensing De novo Peptides Targeting LasR of Pseudomonas aeruginosa.Probiotics and antimicrobial proteins · 2026Article
- Protein adsorption at material interface: mechanistic design framework for engineering ceramic scaffolds for bone repair applications.Biomedical engineering online · 2026Review
- Evolutionary Patterns of the Genes Involved in the Integrity and Segregation of Chromosomes in Sawflies (Hymenoptera: Symphyta).Ecology and evolution · 2026Article
- Article
- Structure-Based De Novo Design for the Discovery of Miniprotein Inhibitors Targeting Oncogenic Mutant BRAF.International journal of molecular sciences · 2024Article
- Article
- Development of themSphere · 2023Article
- Main Factors Shaping Amino Acid Usage Across Evolution.Journal of molecular evolution · 2023Review
- A novel strategy for developing vaccine candidate against Jaagsiekte sheep retrovirus from the envelope and gag proteins: an in-silico approach.BMC veterinary research · 2022Article
- How Honey Bee Vitellogenin Holds Lipid Cargo: A Role for the C-Terminal.Frontiers in molecular biosciences · 2022Article
- In Silico Modeling of the Influence of Environment on Amyloid Folding Using FOD-M Model.International journal of molecular sciences · 2021Article
Corrections and comments
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Authors and funding
6 authors.
Funding
Abstract
Protein solubility is based on the compatibility of the specific protein surface with the polar aquatic environment. The exposure of polar residues to the protein surface promotes the protein's solubility in the polar environment. The aquatic environment also influences the folding process by favoring the centralization of hydrophobic residues with the simultaneous exposure to polar residues. The degree of compatibility of the residue distribution, with the model of the concentration of hydrophobic residues in the center of the molecule, with the simultaneous exposure of polar residues is determined by the sequence of amino acids in the chain. The fuzzy oil drop model enables the quantification of the degree of compatibility of the hydrophobicity distribution observed in the protein to a form fully consistent with the Gaussian 3D function, which expresses an idealized distribution that meets the preferences of the polar water environment. The varied degrees of compatibility of the distribution observed with the idealized one allow the prediction of preferences to interactions with molecules of different polarity, including water molecules in particular. This paper analyzes a set of proteins with different levels of hydrophobicity distribution in the context of the solubility of a given protein and the possibility of complex formation.
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