How wide is the window opened by high-resolution relaxometry on the internal dynamics of proteins in solution?
Abstract
The dynamics of molecules in solution is usually quantified by the determination of timescale-specific amplitudes of motions. High-resolution nuclear magnetic resonance (NMR) relaxometry experiments—where the sample is transferred to low fields for longitudinal (T1) relaxation, and back to high field for detection with residue-specific resolution—seeks to increase the ability to distinguish the contributions from motion on timescales slower than a few nanoseconds. However, tumbling of a molecule in solution masks some of these motions. Therefore, we investigate to what extent relaxometry improves timescale resolution, using the “detector” analysis of dynamics. Here, we demonstrate improvements in the characterization of internal dynamics of methyl-bearing side chains by carbon-13 relaxometry in the small protein ubiquitin. We show that relaxometry data leads to better information about nanosecond motions as compared to high-field relaxation data only. Our calculations show that gains from relaxometry are greater with increasing correlation time of rotational diffusion. Show more
Permanent link
https://doi.org/10.3929/ethz-b-000478960Publication status
publishedExternal links
Journal / series
Journal of Biomolecular NMRVolume
Pages / Article No.
Publisher
SpringerSubject
Dynamics; Relaxometry; Detector analysis; Solution-state NMROrganisational unit
03496 - Meier, Beat H. (emeritus) / Meier, Beat H. (emeritus)
08829 - Ernst, Matthias (Tit.-Prof.)
Funding
899683 - FET Open – Novel ideas for radically new technologies (EC)
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