ArticleThe journal of physical chemistry. B2025
Computing the pH-Dependent Thermodynamics of the Allostery between Dimerization and Palmitate Binding in β-Lactoglobulin.
Article in The journal of physical chemistry. B, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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1 citing paper in PubMed.
- Quantifying the Acidification-Induced Shift of the Dimerization Equilibrium of PsbS.The journal of physical chemistry letters · 2026Article
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3 authors.
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Abstract
The study of pH-dependent allosteric processes presents a significant challenge, both experimentally and computationally. In this work, we apply the constant-pH molecular dynamics method to explore an interesting case of allostery involving protein-ligand binding and dimerization. As a model system, we use β-lactoglobulin (BLG), a small protein from bovine milk known to dimerize and bind palmitic acid in a hydrophobic pocket─both processes sensitive to pH. This study focuses on the holo form of BLG, and, when combined with our previous study of the apo form (da Rocha et al.
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