What is it about?
Hydration shell properties in proteins continue to be an active topic of investigation due to their complexity and importance for biological processes. This work explores how water molecules move around protein surfaces as well as interactions between different hydration layers. We investigate proteins in their highly concentrated solid or gel-like phases over a very broad temperature range from room temperature down to -150 F (170 K). We find that protein molecules remain mobile at the protein surface even at these low temperatures. We thus devise specific models of how they move and interact with each other. The details of mobility of the hydration layers are important for functions such as protein-protein interactions, drug-protein interactions, and interactions with other molecular components within the cell.
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Perspectives
We hope this article will raise awareness of how fundamental research in chemistry and physics can eventually facilitate discoveries in biomedical applications. Water remains the most mysterious molecule on Earth. L.V. dedicates this paper to her father Boris E. Vugmeister, a well-known solid-state physicist, who passed away while the manuscript was written: to my father, who taught me what science means.
Liliya Vugmeyster
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This page is a summary of: Multi-mode water dynamics in hydration shells of villin headpiece subdomain protein in the solid state using deuterium and oxygen-17 NMR spectroscopy, The Journal of Chemical Physics, July 2025, American Institute of Physics,
DOI: 10.1063/5.0279081.
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