ArticleAngewandte Chemie (International ed. in English)2015
A sharp thermal transition of fast aromatic-ring dynamics in ubiquitin.
Article in Angewandte Chemie (International ed. in English), 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed.
- Genetically Encoded Pentafluorophenylalanine Enables Quantitative Probing of Local Protein Malleability by 19F NMR.Journal of the American Chemical Society · 2026Article
- Article
- Free-Energy Landscape and Rate Estimation of the Aromatic Ring Flips in Basic Pancreatic Trypsin Inhibitors Using Metadynamics.Journal of chemical theory and computation · 2023Article
- NMR Studies of Aromatic Ring Flips to Probe Conformational Fluctuations in Proteins.The journal of physical chemistry. B · 2023Review
- Aromatic ring flips in differently packed ubiquitin protein crystals from MAS NMR and MD.Journal of structural biology: X · 2023Article
- Characterizing Fast Conformational Exchange of Aromatic Rings Using Residual Dipolar Couplings: Distinguishing Jumplike Flips from Other Exchange Mechanisms.The journal of physical chemistry. B · 2022Article
- Article
- Transition-State Compressibility and Activation Volume of Transient Protein Conformational Fluctuations.JACS Au · 2021Article
- Protein conformational entropy is not slaved to water.Scientific reports · 2020Article
- Slow ring flips in aromatic cluster of GB1 studied by aromaticJournal of biomolecular NMR · 2020Article
- Structure and Dynamics of Stacking Interactions in an Antibody Binding Site.Biochemistry · 2019Article
- Conformational exchange of aromatic side chains byJournal of biomolecular NMR · 2018Article
- Phenyl-Ring Dynamics in Amyloid Fibrils and Proteins: The Microscopic-Order-Macroscopic-Disorder Perspective.The journal of physical chemistry. B · 2018Article
- Practical aspects of high-pressure NMR spectroscopy and its applications in protein biophysics and structural biology.Methods (San Diego, Calif.) · 2018Article
- Late metabolic precursors for selective aromatic residue labeling.Journal of biomolecular NMR · 2018Review
- Site-selectiveJournal of biomolecular NMR · 2017Article
- Anthranilic acid, the new player in the ensemble of aromatic residue labeling precursor compounds.Journal of biomolecular NMR · 2017Article
- Solvent-Driven Dynamical Crossover in the Phenylalanine Side-Chain from the Hydrophobic Core of Amyloid Fibrils Detected byThe journal of physical chemistry. B · 2017Article
- Site-selectiveJournal of biomolecular NMR · 2017Article
- A dynamic look backward and forward.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2016Review
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Authors and funding
4 authors.
Funding
Abstract
Aromatic amino acid side chains have a rich role within proteins and are often central to their structure and function. Suitable isotopic-labelling strategies enable studies of sub-nanosecond aromatic-ring dynamics using solution NMR relaxation methods. Surprisingly, it was found that the three aromatic side chains in human ubiquitin show a sharp thermal dynamical transition at approximately 312 K. Hydrostatic pressure has little effect on the low-temperature behavior, but somewhat decreases the amplitude of motion in the high-temperature regime. Therefore, below the transition temperature, ring motion is largely librational. Above this temperature, a complete ring-rotation process that is fully consistent with a continuous diffusion not requiring the transient creation of a large activated free volume occurs. Molecular dynamics simulations qualitatively corroborate this view and reinforce the notion that the dynamical character of the protein interior has much more liquid-alkane-like properties than previously appreciated.
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