ArticleJournal of the American Chemical Society2020
Ultrafast Dynamics of Water-Protein Coupled Motions around the Surface of Eye Crystallin.
Article in Journal of the American Chemical Society, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
What it found
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Who cites it
8 citing papers in PubMed, 26 citations in OpenAlex.
- Changes in Water Dynamics by Osmolytes Regulate Enzyme Activity.The journal of physical chemistry. B · 2026Article
- Interplay of protein fluctuation and associated water dynamics in osmolyte-induced stabilization.Biophysical journal · 2025Article
- Residue-Specific Structural and Dynamical Coupling of Protein and Hydration Water Revealed by Molecular Dynamics Simulations.Biomolecules · 2025Article
- Contrasting Changes in Strongly and Weakly Bound Hydration Water of a Protein upon Denaturation.The journal of physical chemistry. B · 2023Article
- Heterogeneous and Allosteric Role of Surface Hydration for Protein-Ligand Binding.Journal of chemical theory and computation · 2023Article
- Environment-Driven Coherent Population Transfer Governs the Ultrafast Photophysics of Tryptophan.Journal of the American Chemical Society · 2022Article
- Slowdown of Water Dynamics from the Top to the Bottom of the GroEL Cavity.The journal of physical chemistry letters · 2021Article
- Chemical Properties Determine Solubility and Stability in βγ-Crystallins of the Eye Lens.Chembiochem : a European journal of chemical biology · 2021Review
Corrections and comments
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Authors and funding
8 authors at 1 institution in 1 country.
Funding
Abstract
Water dynamics on the protein surface mediate both protein structure and function. However, many questions remain about the role of the protein hydration layers in protein fluctuations and how the dynamics of these layers relate to specific protein properties. The fish eye lens protein γM7-crystallin (γM7) is found in vivo at extremely high concentrations nearing the packing limit, corresponding to only a few water layers between adjacent proteins. In this study, we conducted a site-specific probing of hydration water motions and side-chain dynamics at nine selected sites around the surface of γM7 using a tryptophan scan with femtosecond spectroscopy and NMR nuclear spin relaxation (NSR). We observed correlated fluctuations between hydration water and protein side chains on the time scales of a few picoseconds and hundreds of picoseconds, corresponding to local reorientations and network restructuring, respectively. These motions are heterogeneous over the protein surface and relate to the various steric and chemical properties of the local protein environment. Overall, we found that γM7 has relatively slower water dynamics within the hydration shell than a similar β-sheet protein, which may contribute to the high packing limit of this unique protein.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.