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

revised on 11.09.2019 and posted on 11.09.2019 by Pavel Kaderavek, Nicolas Bolik-Coulon, Samuel Cousin, Thorsten Marquardsen, Jean-Max Tyburn, Jean-Nicolas Dumez, Fabien Ferrage

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.


ERC Grant agreement 279519 (2F4BIODYN)


Email Address of Submitting Author


École normale supérieure, PSL University, Sorbonne Université, CNRS



ORCID For Submitting Author


Declaration of Conflict of Interest

TM and JMT are employees of Bruker Biospin