ArticleScientific reports2018
Computational analysis of the amino acid interactions that promote or decrease protein solubility.
Article in Scientific reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 77 citations in OpenAlex.
- Strategies for enhancing protein solubility: methods, applications, and prospects.NPJ science of food · 2026Review
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- Genome-wide systematic characterization of PHT gene family and its member involved in phosphate uptake in Orychophragmus violaceus.BMC genomics · 2025Article
- PInteract: Detecting Aromatic-Involving Motifs in Proteins and Protein-Nucleic Acid Complexes.Biomolecules · 2025Article
- SOuLMuSiC, a novel tool for predicting the impact of mutations on protein solubility.Scientific reports · 2025Article
- Ionome mapping and amino acid metabolome profiling of Phaseolus vulgaris L. seeds imbibed with computationally informed phytoengineered copper sulphide nanoparticles.Discover nano · 2024Article
- Ostrinia furnacalis PBP2 solution NMR structure: Insight into ligand binding and release mechanisms.Protein science : a publication of the Protein Society · 2022Article
- Mutational dynamics across VOCs in International travellers and Community transmission underscores importance of Spike-ACE2 interaction.Microbiological research · 2022Article
- Helix 8 in chemotactic receptors of the complement system.PLoS computational biology · 2022Article
- Characterization of gliadin, secalin and hordein fractions using analytical techniques.Scientific reports · 2021Article
- TISIGNER.com: web services for improving recombinant protein production.Nucleic acids research · 2021Article
- Solubility and Aggregation of Selected Proteins Interpreted on the Basis of Hydrophobicity Distribution.International journal of molecular sciences · 2021Article
- Characterization and Quantitative Determination of a Diverse Group of Bacillus subtilis subsp. subtilis NCIB 3610 Antibacterial Peptides.Probiotics and antimicrobial proteins · 2021Article
- Ru-containing magnetic yolk-shell structured nanocomposite: a powerful, recoverable and highly durable nanocatalyst.RSC advances · 2021Article
- Toward complete rational control over protein structure and function through computational design.Current opinion in structural biology · 2021Review
- BRANEart: Identify Stability Strength and Weakness Regions in Membrane Proteins.Frontiers in bioinformatics · 2021Article
- Melting properties of amino acids and their solubility in water.RSC advances · 2020Article
- Investigation of Supercharging as A Strategy to Enhance the Solubility and Plasminogen Cleavage Activity of Reteplase.Iranian journal of biotechnology · 2020Article
- Solubility-Weighted Index: fast and accurate prediction of protein solubility.Bioinformatics (Oxford, England) · 2020Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The solubility of globular proteins is a basic biophysical property that is usually a prerequisite for their functioning. In this study, we probed the solubility of globular proteins with the help of the statistical potential formalism, in view of objectifying the connection of solubility with structural and energetic properties and of the solubility-dependence of specific amino acid interactions. We started by setting up two independent datasets containing either soluble or aggregation-prone proteins with known structures. From these two datasets, we computed solubility-dependent distance potentials that are by construction biased towards the solubility of the proteins from which they are derived. Their analysis showed the clear preference of amino acid interactions such as Lys-containing salt bridges and aliphatic interactions to promote protein solubility, whereas others such as aromatic, His-π, cation-π, amino-π and anion-π interactions rather tend to reduce it. These results indicate that interactions involving delocalized π-electrons favor aggregation, unlike those involving no (or few) dispersion forces. Furthermore, using our potentials derived from either highly or weakly soluble proteins to compute protein folding free energies, we found that the difference between these two energies correlates better with solubility than other properties analyzed before such as protein length, isoelectric point and aliphatic index. This is, to the best of our knowledge, the first comprehensive in silico study of the impact of residue-residue interactions on protein solubility properties.The results of this analysis provide new insights that will facilitate future rational protein design applications aimed at modulating the solubility of targeted proteins.
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