| JASEŇÁKOVÁ, Zuzana, Vojtěch ZAPLETAL, Petr PADRTA, Milan ZACHRDLA, N. BOLIK-COULON, T. MARQUARDSEN, J.M. TYBURN, Lukáš ŽÍDEK, F. FERRAGE a Pavel KADEŘÁVEK. Boosting the resolution of low-field 15N relaxation experiments on intrinsically disordered proteins with triple-resonance NMR. Journal of biomolecular NMR. Dordrecht: Springer, 2020, roč. 74, 2-3, s. 139-145. ISSN 0925-2738. Dostupné z: https://dx.doi.org/10.1007/s10858-019-00298-6. |
Další formáty:
BibTeX
LaTeX
RIS
@article{1655339,
author = {Jaseňáková, Zuzana and Zapletal, Vojtěch and Padrta, Petr and Zachrdla, Milan and BolikandCoulon, N. and Marquardsen, T. and Tyburn, J.M. and Žídek, Lukáš and Ferrage, F. and Kadeřávek, Pavel},
article_location = {Dordrecht},
article_number = {2-3},
doi = {http://dx.doi.org/10.1007/s10858-019-00298-6},
keywords = {Nuclear magnetic resonance; Relaxation; Dynamics; Intrinsically disordered proteins; High-resolution relaxometry; Non-uniform sampling},
language = {eng},
issn = {0925-2738},
journal = {Journal of biomolecular NMR},
title = {Boosting the resolution of low-field 15N relaxation experiments on intrinsically disordered proteins with triple-resonance NMR},
url = {https://link.springer.com/article/10.1007%2Fs10858-019-00298-6},
volume = {74},
year = {2020}
}
TY - JOUR
ID - 1655339
AU - Jaseňáková, Zuzana - Zapletal, Vojtěch - Padrta, Petr - Zachrdla, Milan - Bolik-Coulon, N. - Marquardsen, T. - Tyburn, J.M. - Žídek, Lukáš - Ferrage, F. - Kadeřávek, Pavel
PY - 2020
TI - Boosting the resolution of low-field 15N relaxation experiments on intrinsically disordered proteins with triple-resonance NMR
JF - Journal of biomolecular NMR
VL - 74
IS - 2-3
SP - 139-145
EP - 139-145
PB - Springer
SN - 09252738
KW - Nuclear magnetic resonance
KW - Relaxation
KW - Dynamics
KW - Intrinsically disordered proteins
KW - High-resolution relaxometry
KW - Non-uniform sampling
UR - https://link.springer.com/article/10.1007%2Fs10858-019-00298-6
L2 - https://link.springer.com/article/10.1007%2Fs10858-019-00298-6
N2 - 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 15Namide 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 delta subunit of RNA polymerase from Bacillus subtilis, a protein with highly repetitive amino-acid sequence and very low dispersion of backbone chemical shifts.
ER -
JASEŇÁKOVÁ, Zuzana, Vojtěch ZAPLETAL, Petr PADRTA, Milan ZACHRDLA, N. BOLIK-COULON, T. MARQUARDSEN, J.M. TYBURN, Lukáš ŽÍDEK, F. FERRAGE a Pavel KADEŘÁVEK. Boosting the resolution of low-field 15N relaxation experiments on intrinsically disordered proteins with triple-resonance NMR. \textit{Journal of biomolecular NMR}. Dordrecht: Springer, 2020, roč.~74, 2-3, s.~139-145. ISSN~0925-2738. Dostupné z: https://dx.doi.org/10.1007/s10858-019-00298-6.
|
