ArticleJournal of the American Chemical Society2011
Site-specific hydration dynamics in the nonpolar core of a molten globule by dynamic nuclear polarization of water.
Article in Journal of the American Chemical Society, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.
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Who cites it
39 citing papers in PubMed, 103 citations in OpenAlex.
- Thermally activated coupling between protein vibrations and interfacial water dynamics revealed by terahertz spectroscopy.iScience · 2026Article
- 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 · 2025Article
- Water inside the Selectivity Filter of a KJournal of the American Chemical Society · 2024Article
- Design of Soft Material Surfaces with Rationally Tuned Water Diffusivity.ACS central science · 2023Article
- Heterogeneous and Allosteric Role of Surface Hydration for Protein-Ligand Binding.Journal of chemical theory and computation · 2023Article
- Toward protein NMR at physiological concentrations by hyperpolarized water-Finding and mapping uncharted conformational spaces.Science advances · 2022Article
- The Molten Globule State of a Globular Protein in a Cell Is More or Less Frequent Case Rather than an Exception.Molecules (Basel, Switzerland) · 2022Review
- Hyperpolarized water as universal sensitivity booster in biomolecular NMR.Nature protocols · 2022Review
- Fluorescence Anisotropy Decays and Microscale-Volume Viscometry Reveal the Compaction of Ribosome-Bound Nascent Proteins.The journal of physical chemistry. B · 2021Article
- Challenges and Advances in the Application of Dynamic Nuclear Polarization to Liquid-State NMR Spectroscopy.The journal of physical chemistry. B · 2021Review
- Real-time tracking of protein unfolding with time-resolved x-ray solution scattering.Structural dynamics (Melville, N.Y.) · 2020Article
- Article
- Solvent-dependent segmental dynamics in intrinsically disordered proteins.Science advances · 2019Article
- Protein Solvent Shell Structure Provides Rapid Analysis of Hydration Dynamics.Journal of chemical information and modeling · 2019Article
- Entropy connects water structure and dynamics in protein hydration layer.Physical chemistry chemical physics : PCCP · 2018Article
- Slow Dynamics around a Protein and Its Coupling to Solvent.ACS central science · 2018Article
- Spatially Heterogeneous Surface Water Diffusivity around Structured Protein Surfaces at Equilibrium.Journal of the American Chemical Society · 2017Article
- The dynamics of peptide-water interactions in dialanine: An ultrafast amide I 2D IR and computational spectroscopy study.The Journal of chemical physics · 2017Article
- Article
- Hydration Dynamics of a Peripheral Membrane Protein.Journal of the American Chemical Society · 2016Article
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
Abstract
Water-protein interactions play a direct role in protein folding. The chain collapse that accompanies protein folding involves extrusion of water from the nonpolar core. For many proteins, including apomyoglobin (apoMb), hydrophobic interactions drive an initial collapse to an intermediate state before folding to the final structure. However, the debate continues as to whether the core of the collapsed intermediate state is hydrated and, if so, what the dynamic nature of this water is. A key challenge is that protein hydration dynamics is significantly heterogeneous, yet suitable experimental techniques for measuring hydration dynamics with site-specificity are lacking. Here, we introduce Overhauser dynamic nuclear polarization at 0.35 T via site-specific nitroxide spin labels as a unique tool to probe internal and surface protein hydration dynamics with site-specific resolution in the molten globular, native, and unfolded protein states. The (1)H NMR signal enhancement of water carries information about the local dynamics of the solvent within ∼10 Å of a spin label. EPR is used synergistically to gain insights on local polarity and mobility of the spin-labeled protein. Several buried and solvent-exposed sites of apoMb are examined, each bearing a covalently bound nitroxide spin label. We find that the nonpoloar core of the apoMb molten globule is hydrated with water bearing significant translational dynamics, only 4-6-fold slower than that of bulk water. The hydration dynamics of the native state is heterogeneous, while the acid-unfolded state bears fast-diffusing hydration water. This study provides a high-resolution glimpse at the folding-dependent nature of protein hydration dynamics.
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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.