ArticleJournal of the American Chemical Society2013
Nanosecond time scale motions in proteins revealed by high-resolution NMR relaxometry.
Article in Journal of the American Chemical Society, 2013. 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.
- High-Resolution Relaxometry for Fragment Screening.Journal of medicinal chemistry · 2026Article
- Single-scan detection of ligand-binding using hyperpolarization and low-field relaxation.Communications chemistry · 2026Article
- A steady-state approach for analysis of high-resolution relaxometry.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2025Article
- Extending the detectable time window of fast protein dynamics usingJournal of biomolecular NMR · 2025Article
- Extracting Trends From NMR Data With TrAGICo: A Python Toolbox.Magnetic resonance in chemistry : MRC · 2025Article
- A fast sample shuttle to couple high and low magnetic fields and applications in high-resolution relaxometry.Magnetic resonance (Gottingen, Germany) · 2025Article
- Using NMR diffusion data to validate MD models of disordered proteins: Test case of N-terminal tail of histone H4.Biophysical journal · 2024Article
- A dual-core NMR system for field-cycling singlet assisted diffusion NMR.Frontiers in chemistry · 2023Article
- DHFR Mutants Modulate Their Synchronized Dynamics with the Substrate by Shifting Hydrogen Bond Occupancies.Journal of chemical information and modeling · 2022Article
- Convergent views on disordered protein dynamics from NMR and computational approaches.Biophysical journal · 2022Article
- Nanobody Paratope Ensembles in Solution Characterized by MD Simulations and NMR.International journal of molecular sciences · 2022Article
- Conformational Dynamics of Intrinsically Disordered Proteins Regulate Biomolecular Condensate Chemistry.Chemical reviews · 2022Review
- High ResolutionFrontiers in molecular biosciences · 2022Review
- How wide is the window opened by high-resolution relaxometry on the internal dynamics of proteins in solution?Journal of biomolecular NMR · 2021Article
- Impact of the Solvent Quality on the Local Dynamics of Soft and Swollen Polymer Nanoparticles Functionalized with Polymer Chains.Macromolecules · 2020Article
- Boosting the resolution of low-fieldJournal of biomolecular NMR · 2020Article
- Surprising absence of strong homonuclear coupling at low magnetic field explored by two-field nuclear magnetic resonance spectroscopy.Magnetic resonance (Gottingen, Germany) · 2020Article
- Relaxing with liquids and solids - A perspective on biomolecular dynamics.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2019Review
- Analysis of NMR Spin-Relaxation Data Using an Inverse Gaussian Distribution Function.Biophysical journal · 2018Article
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9 authors.
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Abstract
Understanding the molecular determinants underlying protein function requires the characterization of both structure and dynamics at atomic resolution. Nuclear relaxation rates allow a precise characterization of protein dynamics at the Larmor frequencies of spins. This usually limits the sampling of motions to a narrow range of frequencies corresponding to high magnetic fields. At lower fields one cannot achieve sufficient sensitivity and resolution in NMR. Here, we use a fast shuttle device where the polarization builds up and the signals are detected at high field, while longitudinal relaxation takes place at low fields 0.5 < B0 < 14.1 T. The sample is propelled over a distance up to 50 cm by a blowgun-like system in about 50 ms. The analysis of nitrogen-15 relaxation in the protein ubiquitin over such a wide range of magnetic fields offers unprecedented insights into molecular dynamics. Some key regions of the protein feature structural fluctuations on nanosecond time scales, which have so far been overlooked in high-field relaxation studies. Nanosecond motions in proteins may have been underestimated by traditional high-field approaches, and slower supra-τ(c) motions that have no effect on relaxation may have been overestimated. High-resolution relaxometry thus opens the way to a quantitative characterization of nanosecond motions in proteins.
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