Boosting the resolution of low-field 15N relaxation experiments
on intrinsically disordered proteins with triple-resonance NMR

J 2020

Boosting the resolution of low-field 15N relaxation experiments on intrinsically disordered proteins with triple-resonance NMR

JASEŇÁKOVÁ, Zuzana, Vojtěch ZAPLETAL, Petr PADRTA, Milan ZACHRDLA, N. BOLIK-COULON et. al.

Základní údaje

Originální název

Boosting the resolution of low-field 15N relaxation experiments on intrinsically disordered proteins with triple-resonance NMR

Autoři

JASEŇÁKOVÁ, Zuzana (703 Slovensko, domácí), Vojtěch ZAPLETAL (203 Česká republika, domácí), Petr PADRTA (203 Česká republika, domácí), Milan ZACHRDLA (203 Česká republika), N. BOLIK-COULON, T. MARQUARDSEN, J.M. TYBURN, Lukáš ŽÍDEK (203 Česká republika, domácí), F. FERRAGE a Pavel KADEŘÁVEK (203 Česká republika, garant, domácí)

Vydání

Journal of biomolecular NMR, Dordrecht, Springer, 2020, 0925-2738

Další údaje

Jazyk

angličtina

Typ výsledku

Článek v odborném periodiku

Obor

10608 Biochemistry and molecular biology

Stát vydavatele

Nizozemské království

Utajení

není předmětem státního či obchodního tajemství

Odkazy

URL

Impakt faktor

Impact factor: 2.835

Kód RIV

RIV/00216224:14740/20:00114136

Organizační jednotka

Středoevropský technologický institut

DOI

http://dx.doi.org/10.1007/s10858-019-00298-6

UT WoS

000520461300004

Klíčová slova anglicky

Nuclear magnetic resonance; Relaxation; Dynamics; Intrinsically disordered proteins; High-resolution relaxometry; Non-uniform sampling

Štítky

rivok

Příznaky

Mezinárodní význam, Recenzováno

Změněno: 30. 10. 2024 14:13, Ing. Martina Blahová

Anotace

V originále

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.

Návaznosti

GJ18-04197Y, projekt VaV

Název: Charakterizace flexibilních oblastí RNA polymerázy Bacillus subtilis

Investor: Grantová agentura ČR, Characterization of dynamical regions in RNA polymerase from Bacillus subtilis

90127, velká výzkumná infrastruktura

Název: CIISB II

Citovat

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.

@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.

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