Boosting the resolution of low-field 15 N relaxation experiments on intrinsically disordered proteins with triple-resonance NMR
Language English Country Netherlands Media print-electronic
Document type Journal Article
Grant support
GA18-04197Y
Grantová Agentura České Republiky
ANR-18-CE29-0003
Agence Nationale de la Recherche
CA15209
European Cooperation in Science and Technology
PubMed
31960224
DOI
10.1007/s10858-019-00298-6
PII: 10.1007/s10858-019-00298-6
Knihovny.cz E-resources
- Keywords
- Dynamics, High-resolution relaxometry, Intrinsically disordered proteins, Non-uniform sampling, Nuclear magnetic resonance, Relaxation,
- MeSH
- Bacillus subtilis enzymology MeSH
- Bacterial Proteins chemistry MeSH
- DNA-Directed RNA Polymerases chemistry MeSH
- Nuclear Magnetic Resonance, Biomolecular * MeSH
- Recombinant Proteins chemistry MeSH
- Intrinsically Disordered Proteins chemistry MeSH
- Publication type
- Journal Article MeSH
- Names of Substances
- Bacterial Proteins MeSH
- DNA-Directed RNA Polymerases MeSH
- Recombinant Proteins MeSH
- Intrinsically Disordered Proteins MeSH
Improving our understanding of nanosecond motions in disordered proteins requires the enhanced sampling of the spectral density function obtained from relaxation at low magnetic fields. High-resolution relaxometry and two-field NMR measurements of relaxation have, so far, only been based on the recording of one- or two-dimensional spectra, which provide insufficient resolution for challenging disordered proteins. Here, we introduce a 3D-HNCO-based two-field NMR experiment for measurements of protein backbone 15 N amide longitudinal relaxation rates. The experiment provides accurate longitudinal relaxation rates at low field (0.33 T in our case) preserving the resolution and sensitivity typical for high-field NMR spectroscopy. Radiofrequency pulses applied on six different radiofrequency channels are used to manipulate the spin system at both fields. The experiment was demonstrated on the C-terminal domain of δ subunit of RNA polymerase from Bacillus subtilis, a protein with highly repetitive amino-acid sequence and very low dispersion of backbone chemical shifts.
Bruker BioSpin 34 rue de l'Industrie BP 10002 67166 Wissembourg Cedex France
Bruker BioSpin GmbH Silberstreifen 4 76287 Rheinstetten Germany
Central European Institute of Technology Masaryk University Kamenice 5 625 00 Brno Czech Republic
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