ArticleInternational journal of molecular sciences2024
Correlation of Solvent Interaction Analysis Signatures with Thermodynamic Properties and In Silico Calculations of the Structural Effects of Point Mutations in Two Proteins.
Article in International journal of molecular sciences, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
6 citing papers in PubMed.
- Solvent Interaction Analysis: A New Lens for Protein Structure and Diagnostics.International journal of molecular sciences · 2026Review
- Disrupting virulence: in silico discovery of MexL inhibitors to block pyocyanin biosynthesis in Pseudomonas aeruginosa.Archives of microbiology · 2026Article
- Network pharmacology analysis and cellular experiment validation of puerarin in attenuating TBI through suppression of ferroptosis.Scientific reports · 2026Article
- Article
- Effects of Inorganic Salts on Phase Separation in Aqueous Solutions of Poly(ethylene glycol).International journal of molecular sciences · 2025Article
- Article
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Authors and funding
4 authors.
Funding
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Abstract
The partition behavior of single and double-point mutants of bacteriophage T4 lysozyme (T4 lysozyme) and staphylococcal nuclease A was examined in different aqueous two-phase systems (ATPSs) and studied by Solvent Interaction Analysis (SIA). Additionally, the solvent accessible surface area (SASA) of modeled mutants of both proteins was calculated. The in silico calculations and the in vitro analyses of the staphylococcal nuclease and T4 lysozyme mutants correlate, indicating that the partition analysis in ATPSs provides a valid descriptor (SIA signature) covering various protein features, such as structure, structural dynamics, and conformational stability.
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