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- W3204837760 abstract "<div><div><div><p>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.</p></div></div></div>" @default.
- W3204837760 created "2021-10-11" @default.
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- W3204837760 date "2019-09-11" @default.
- W3204837760 modified "2023-09-25" @default.
- W3204837760 title "Protein Dynamics from Accurate Low-Field Site-Specific Longitudinal and Transverse Relaxation" @default.
- W3204837760 doi "https://doi.org/10.26434/chemrxiv.8850320.v2" @default.
- W3204837760 hasPublicationYear "2019" @default.
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