| Autor: |
Zuzana, Jaseňáková, Vojtěch, Zapletal, Petr, Padrta, Milan, Zachrdla, Nicolas, Bolik-Coulon, Thorsten, Marquardsen, Jean-Max, Tyburn, Lukáš, Žídek, Fabien, Ferrage, Pavel, Kadeřávek |
| Rok vydání: |
2019 |
| Předmět: |
|
| Zdroj: |
Journal of biomolecular NMR. 74(2-3) |
| ISSN: |
1573-5001 |
| Popis: |
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 [Formula: see text] 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 [Formula: see text] subunit of RNA polymerase from Bacillus subtilis, a protein with highly repetitive amino-acid sequence and very low dispersion of backbone chemical shifts. |
| Databáze: |
OpenAIRE |
| Externí odkaz: |
|
Full text from SpringerLink