ArticleThe journal of physical chemistry. A2025
Roles of Hydration in Protein-Ligand Binding: Passive or Active Participant?
Article in The journal of physical chemistry. A, 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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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
1 citing paper in PubMed.
- Solution Phase Protein Dynamics: Influences of ESI Buffers on Hydration.Analytical chemistry · 2026Article
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Authors and funding
7 authors.
Funding
Abstract
Hydration is a critical yet often underappreciated factor that influences protein dynamics in solution, with direct effects on structure, stability, and interactions such as ligand binding. Native mass spectrometry (nMS) enables the analysis of biomolecules in their solution states, which are shaped by cofactors, osmolytes, ligands, and notably, hydration. Here, we employ variable-temperature electrospray ionization to address a central question in molecular biophysics: does hydration act as a passive background solvent or as an active participant in modulating ligand binding? To investigate these effects, temperature-dependent changes in average charge state (
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Registered trials
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