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

Article in a journal

Field of Study

10608 Biochemistry and molecular biology

Country of publisher

Netherlands

Confidentiality degree

is not subject to a state or trade secret

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

EID Scopus

2-s2.0-85078226018

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

Cite

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.

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