ArticlePloS one2012
Protein linewidth and solvent dynamics in frozen solution NMR.
Article in PloS one, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.
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Who cites it
36 citing papers in PubMed.
- Encapsulation of Phytochrome Proteins in Trehalose Matrices: Practical Considerations for the Use in Solid-State NMR Spectroscopy.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Quantifying the liquid-liquid transition in cold water/glycerol mixtures by intermolecular hyperfine relaxation-induced dipolar modulation enhancement (ih-RIDME).Physical chemistry chemical physics : PCCP · 2025Article
- Assignment-Free Determination of Ligand Binding Sites in Proteins by Solid-State NMR.Journal of the American Chemical Society · 2025Article
- Isoleucine Side Chains as Reporters of Conformational Freedom in Protein Folding Studied by DNP-Enhanced NMR.Journal of the American Chemical Society · 2025Article
- Structural Context Modulates the Conformational Ensemble of the Intrinsically Disordered Amino Terminus of α-Synuclein.Journal of the American Chemical Society · 2025Article
- In cell NMR reveals cells selectively amplify and structurally remodel amyloid fibrils.bioRxiv : the preprint server for biology · 2024Article
- Sorbitol-Based Glass Matrices Enable Dynamic Nuclear Polarization beyond 200 K.The journal of physical chemistry letters · 2024Article
- Resolution in cryogenic solid state NMR: Challenges and solutions.Protein science : a publication of the Protein Society · 2024Review
- Cholesterol Biases the Conformational Landscape of the Chemokine Receptor CCR3: A MAS SSNMR-Filtered Molecular Dynamics Study.Journal of chemical information and modeling · 2023Article
- Conformational ensembles explain NMR spectra of frozen intrinsically disordered proteins.Protein science : a publication of the Protein Society · 2023Article
- Temperature as a modulator of allosteric motions and crosstalk in mesophilic and thermophilic enzymes.Frontiers in molecular biosciences · 2023Review
- Characterization of conformational heterogeneity via higher-dimensionality, proton-detected solid-state NMR.Journal of biomolecular NMR · 2022Article
- Nucleic acid-protein interfaces studied by MAS solid-state NMR spectroscopy.Journal of structural biology: X · 2022Article
- NMR techniques in studying water in biotechnological systems.Biophysical reviews · 2020Review
- Targetable Tetrazine-Based Dynamic Nuclear Polarization Agents for Biological Systems.Chembiochem : a European journal of chemical biology · 2020Article
- Advances in studying protein disorder with solid-state NMR.Solid state nuclear magnetic resonance · 2020Review
- Article
- Dynamic Nuclear Polarization Magic-Angle Spinning Nuclear Magnetic Resonance Combined with Molecular Dynamics Simulations Permits Detection of Order and Disorder in Viral Assemblies.The journal of physical chemistry. B · 2019Article
- DNP-Enhanced MAS NMR: A Tool to Snapshot Conformational Ensembles of α-Synuclein in Different States.Biophysical journal · 2018Article
- N,N-Diethylmethylamine as lineshape standard for NMR above 130 K.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2018Article
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3 authors.
Funding
Abstract
Solid-state NMR of proteins in frozen aqueous solution is a potentially powerful technique in structural biology, especially if it is combined with dynamic nuclear polarization signal enhancement strategies. One concern regarding NMR studies of frozen solution protein samples at low temperatures is that they may have poor linewidths, thus preventing high-resolution studies. To learn more about how the solvent shell composition and temperature affects the protein linewidth, we recorded ¹H, ²H, and ¹³C spectra of ubiquitin in frozen water and frozen glycerol-water solutions at different temperatures. We found that the ¹³C protein linewidths generally increase with decreasing temperature. This line broadening was found to be inhomogeneous and independent of proton decoupling. In pure water, we observe an abrupt line broadening with the freezing of the bulk solvent, followed by continuous line broadening at lower temperatures. In frozen glycerol-water, we did not observe an abrupt line broadening and the NMR lines were generally narrower than for pure water at the same temperature. ¹H and ²H measurements characterizing the dynamics of water that is in exchange with the protein showed that the ¹³C line broadening is relatively independent from the arrest of isotropic water motions.
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