Informace o publikaci

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

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KADEŘÁVEK Pavel BOLIK-COULON N. COUSIN S.F. MARQUARDSEN T. TYBURN J.M. DUMEZ J.N. FERRAGE F.

Druh Článek v odborném periodiku
Časopis / Zdroj Journal of Physical Chemistry Letters
Fakulta / Pracoviště MU

Středoevropský technologický institut

Citace
www https://pubs.acs.org/doi/10.1021/acs.jpclett.9b02233
Doi http://dx.doi.org/10.1021/acs.jpclett.9b02233
Klíčová slova C-13 NMR-SPECTROSCOPY; SIDE-CHAIN DYNAMICS; BACKBONE DYNAMICS; MAGNETIC-RELAXATION; CYCLING DEVICE; LIQUIDS; PROTON; ENHANCEMENT; RELAXOMETRY; COMPLEXES
Popis Nuclear magnetic relaxation provides invaluable quantitative site specific information on the dynamics of complex systems. Determining dynamics on nanosecond time scales 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 side chains 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 time scales, which opens a new window for the determination of site-specific nanosecond motions in complex systems such as proteins.