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

preprint
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.

Funding

ERC Grant agreement 279519 (2F4BIODYN)

History

Email Address of Submitting Author

Fabien.Ferrage@ens.fr

Institution

École normale supérieure, PSL University, Sorbonne Université, CNRS

Country

France

ORCID For Submitting Author

0000-0002-4738-1723

Declaration of Conflict of Interest

TM and JMT are employees of Bruker Biospin

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