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Protein Dynamics from Accurate Low-Field Site-Specific Longitudinal and Transverse Nuclear Spin Relaxation

Abstract : Nuclear magnetic relaxation provides invaluable quantitative site-specific information on the dynamics of complex systems. Determining dynamics on nanosecond timescales requires relaxation measurements at low magnetic fields, incompatible with high-resolution NMR. Here, we use a two-field NMR spectrometer to measure carbon-13 transverse and longitudinal relaxation rates at a field as low as 0.33 T (proton Larmor frequency 14 MHz) in specifically labeled sidechains of the protein ubiquitin. The use of radiofrequency pulses enhances the accuracy of measurements as compared to high-resolution relaxometry approaches, where the sample is moved in the stray field of the superconducting magnet. Importantly, we demonstrate that accurate measurements at a single low magnetic field provide enough information to characterize complex motions on low nanosecond timescales, which opens a new window for the determination of site-specific nanosecond motions in complex systems such as proteins.
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Pavel Kadeřávek, Nicolas Bolik-­coulon, Samuel Cousin, Thorsten Marquardsen, Jean-Max Tyburn, et al.. Protein Dynamics from Accurate Low-Field Site-Specific Longitudinal and Transverse Nuclear Spin Relaxation. Journal of Physical Chemistry Letters, American Chemical Society, 2019, 10 (19), pp.5917-5922. ⟨10.1021/acs.jpclett.9b02233⟩. ⟨hal-02351026⟩

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