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

• DOI: 10.1021/acs.jpclett.9b02233
• Publication Date: 2019-09-11T17:38:40Z
• Authors: Pavel Kadeřávek; Nicolas Bolik-Coulon; Samuel F. Cousin; Thorsten Marquardsen; Jean-Max Tyburn; Jean-Nicolas Dumez; Fabien Ferrage
• Keywords: Nanosecond; Larmor precession; Protein Dynamics; Tracking (education)

Nuclear magnetic relaxation provides invaluable quantitative site-specific information on the dynamics of complex systems. Determining nanosecond time scales requires measurements at low fields incompatible with high-resolution NMR. Here, we use a two-field NMR spectrometer to measure carbon-13 transverse and longitudinal rates field as 0.33 T (proton Larmor frequency 14 MHz) in specifically labeled side chains protein ubiquitin. The radiofrequency pulses enhances accuracy compared relaxometry approaches, where sample is moved stray superconducting magnet. Importantly, demonstrate that accurate single provide enough characterize motions scales, which opens new window for determination systems such proteins.