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.

Basic information

Original name

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

Authors

JASEŇÁKOVÁ, Zuzana (703 Slovakia, belonging to the institution), Vojtěch ZAPLETAL (203 Czech Republic, belonging to the institution), Petr PADRTA (203 Czech Republic, belonging to the institution), Milan ZACHRDLA (203 Czech Republic), N. BOLIK-COULON, T. MARQUARDSEN, J.M. TYBURN, Lukáš ŽÍDEK (203 Czech Republic, belonging to the institution), F. FERRAGE and Pavel KADEŘÁVEK (203 Czech Republic, guarantor, belonging to the institution)

Edition

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

Other information

Language

English

Type of outcome

Článek v odborném periodiku

Field of Study

10608 Biochemistry and molecular biology

Country of publisher

Netherlands

Confidentiality degree

není předmětem státního či obchodního tajemství

References:

URL

Impact factor

Impact factor: 2.835

RIV identification code

RIV/00216224:14740/20:00114136

Organization unit

Central European Institute of Technology

DOI

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

UT WoS

000520461300004

Keywords in English

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

Abstract

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.

Links

GJ18-04197Y, research and development project

Name: Charakterizace flexibilních oblastí RNA polymerázy Bacillus subtilis

Investor: Czech Science Foundation

90127, large research infrastructures

Name: CIISB II

Citovat

JASEŇÁKOVÁ, Zuzana, Vojtěch ZAPLETAL, Petr PADRTA, Milan ZACHRDLA, N. BOLIK-COULON, T. MARQUARDSEN, J.M. TYBURN, Lukáš ŽÍDEK, F. FERRAGE and 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, vol. 74, 2-3, p. 139-145. ISSN 0925-2738. Available from: 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 and 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, vol.~74, 2-3, p.~139-145. ISSN~0925-2738. Available from: https://dx.doi.org/10.1007/s10858-019-00298-6.

Detailed Information on Publication Record