ArticleThe journal of physical chemistry. B2012
Site-specific hydration dynamics of globular proteins and the role of constrained water in solvent exchange with amphiphilic cosolvents.
Article in The journal of physical chemistry. B, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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Who cites it
28 citing papers in PubMed.
- Two-dimensional bond-selective fluorescence spectroscopy: violations of the resonance condition, vibrational cooling rate dispersion, and super-multiplex imaging.Chemical science · 2025Article
- Nitrile Vibrational Lifetimes as Probes of Local Electric Fields.The journal of physical chemistry letters · 2024Article
- Conformational Features and Hydration Dynamics of Proteins in Cosolvents: A Perspective from Computational Approaches.ACS omega · 2023Review
- Interdomain Interactions Modulate the Active Site Dynamics of Human Inducible Nitric Oxide Synthase.The journal of physical chemistry. B · 2022Article
- Cross-Correlated Motions in Azidolysozyme.Molecules (Basel, Switzerland) · 2022Article
- Site-Specific Interrogation of Protein Structure and Stability.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Transparent window 2D IR spectroscopy of proteins.The Journal of chemical physics · 2021Review
- Protein Dynamics by Two-Dimensional Infrared Spectroscopy.Annual review of analytical chemistry (Palo Alto, Calif.) · 2021Article
- Vibrational Spectroscopic Map, Vibrational Spectroscopy, and Intermolecular Interaction.Chemical reviews · 2020Review
- Mechanical Unfolding of Spectrin Repeats Induces Water-Molecule Ordering.Biophysical journal · 2020Article
- Thermostabilization of VPR, a kinetically stable cold adapted subtilase, via multiple proline substitutions into surface loops.Scientific reports · 2020Article
- Protein Solvent Shell Structure Provides Rapid Analysis of Hydration Dynamics.Journal of chemical information and modeling · 2019Article
- Enhancing the signal strength of surface sensitive 2D IR spectroscopy.The Journal of chemical physics · 2019Article
- How Does Solvation Layer Mobility Affect Protein Structural Dynamics?Frontiers in molecular biosciences · 2018Article
- Spatially Heterogeneous Surface Water Diffusivity around Structured Protein Surfaces at Equilibrium.Journal of the American Chemical Society · 2017Article
- Capturing the photo-signaling state of a photoreceptor in a steady-state fashion by binding a transition metal complex.Protein science : a publication of the Protein Society · 2017Article
- Water Dynamics in the Hydration Shells of Biomolecules.Chemical reviews · 2017Review
- Watching Proteins Wiggle: Mapping Structures with Two-Dimensional Infrared Spectroscopy.Chemical reviews · 2017Review
- Enthalpy-entropy compensation: the role of solvation.European biophysics journal : EBJ · 2017Review
- Probing Site-Specific Structural Information of Peptides at Model Membrane Interface In Situ.Journal of the American Chemical Society · 2015Article
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4 authors.
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Abstract
The thermodynamic driving forces for protein folding, association, and function are often determined by protein-water interactions. With a novel covalently bound labeling approach, we have used sensitive vibrational probes, site-selectively conjugated to two lysozyme variants-in conjunction with ultrafast two-dimensional infrared (2D-IR) spectroscopy-to investigate directly the protein-water interface. By probing alternatively a topologically flat, rigid domain and a flexible domain, we find direct experimental evidence for spatially heterogeneous hydration dynamics. The hydration environment around globular proteins can vary from exhibiting bulk-like hydration dynamics to dynamically constrained water, which results from stifled hydrogen bond switching dynamics near extended hydrophobic surfaces. Furthermore, we leverage preferential solvation exchange to demonstrate that the liberation of dynamically constrained water is a sufficient driving force for protein-surface association reactions. These results provide an intuitive picture of the dynamic aspects of hydrophobic hydration of proteins, illustrating an essential function of water in biological processes.
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