Protein Dynamics from Accurate Low-Field Site-Specific
Longitudinal and Transverse Nuclear Spin Relaxation

J 2019

Protein Dynamics from Accurate Low-Field Site-Specific Longitudinal and Transverse Nuclear Spin Relaxation

KADEŘÁVEK, Pavel, N. BOLIK-COULON, S.F. COUSIN, T. MARQUARDSEN, J.M. TYBURN et. al.

Basic information

Original name

Protein Dynamics from Accurate Low-Field Site-Specific Longitudinal and Transverse Nuclear Spin Relaxation

Authors

KADEŘÁVEK, Pavel (203 Czech Republic, guarantor, belonging to the institution), N. BOLIK-COULON, S.F. COUSIN, T. MARQUARDSEN, J.M. TYBURN, J.N. DUMEZ and F. FERRAGE

Edition

Journal of Physical Chemistry Letters, Washington, American Chemical Society, 2019, 1948-7185

Other information

Language

English

Type of outcome

Článek v odborném periodiku

Field of Study

10403 Physical chemistry

Country of publisher

United States of America

Confidentiality degree

není předmětem státního či obchodního tajemství

References:

URL

Impact factor

Impact factor: 6.710

RIV identification code

RIV/00216224:14740/19:00113242

Organization unit

Central European Institute of Technology

DOI

http://dx.doi.org/10.1021/acs.jpclett.9b02233

UT WoS

000489189500037

Keywords in English

C-13 NMR-SPECTROSCOPY; SIDE-CHAIN DYNAMICS; BACKBONE DYNAMICS; MAGNETIC-RELAXATION; CYCLING DEVICE; LIQUIDS; PROTON; ENHANCEMENT; RELAXOMETRY; COMPLEXES

Abstract

V originále

Nuclear magnetic relaxation provides invaluable quantitative site specific information on the dynamics of complex systems. Determining dynamics on nanosecond time scales requires relaxation measurements at low magnetic fields incompatible with high-resolution NMR. Here, we use a two-field NMR spectrometer to measure carbon-13 transverse and longitudinal relaxation rates at a field as low as 0.33 T (proton Larmor frequency 14 MHz) in specifically labeled side chains of the protein ubiquitin. The use of radiofrequency pulses enhances the accuracy of measurements as compared to high-resolution relaxometry approaches, where the sample is moved in the stray field of the superconducting magnet. Importantly, we demonstrate that accurate measurements at a single low magnetic field provide enough information to characterize complex motions on low nanosecond time scales, which opens a new window for the determination of site-specific nanosecond motions in complex systems such as proteins.

Links

90043, large research infrastructures

Name: CIISB

Citovat

KADEŘÁVEK, Pavel, N. BOLIK-COULON, S.F. COUSIN, T. MARQUARDSEN, J.M. TYBURN, J.N. DUMEZ and F. FERRAGE. Protein Dynamics from Accurate Low-Field Site-Specific Longitudinal and Transverse Nuclear Spin Relaxation. Journal of Physical Chemistry Letters. Washington: American Chemical Society, 2019, vol. 10, No 19, p. 5917-5922. ISSN 1948-7185. Available from: https://dx.doi.org/10.1021/acs.jpclett.9b02233.

@article{1635236,
   author = {Kadeřávek, Pavel and BolikandCoulon, N. and Cousin, S.F. and Marquardsen, T. and Tyburn, J.M. and Dumez, J.N. and Ferrage, F.},
   article_location = {Washington},
   article_number = {19},
   doi = {http://dx.doi.org/10.1021/acs.jpclett.9b02233},
   keywords = {C-13 NMR-SPECTROSCOPY; SIDE-CHAIN DYNAMICS; BACKBONE DYNAMICS; MAGNETIC-RELAXATION; CYCLING DEVICE; LIQUIDS; PROTON; ENHANCEMENT; RELAXOMETRY; COMPLEXES},
   language = {eng},
   issn = {1948-7185},
   journal = {Journal of Physical Chemistry Letters},
   title = {Protein Dynamics from Accurate Low-Field Site-Specific Longitudinal and Transverse Nuclear Spin Relaxation},
   url = {https://pubs.acs.org/doi/10.1021/acs.jpclett.9b02233},
   volume = {10},
   year = {2019}
}

TY  - JOUR
ID  - 1635236
AU  - Kadeřávek, Pavel - Bolik-Coulon, N. - Cousin, S.F. - Marquardsen, T. - Tyburn, J.M. - Dumez, J.N. - Ferrage, F.
PY  - 2019
TI  - Protein Dynamics from Accurate Low-Field Site-Specific Longitudinal and Transverse Nuclear Spin Relaxation
JF  - Journal of Physical Chemistry Letters
VL  - 10
IS  - 19
SP  - 5917-5922
EP  - 5917-5922
PB  - American Chemical Society
SN  - 19487185
KW  - C-13 NMR-SPECTROSCOPY
KW  - SIDE-CHAIN DYNAMICS
KW  - BACKBONE DYNAMICS
KW  - MAGNETIC-RELAXATION
KW  - CYCLING DEVICE
KW  - LIQUIDS
KW  - PROTON
KW  - ENHANCEMENT
KW  - RELAXOMETRY
KW  - COMPLEXES
UR  - https://pubs.acs.org/doi/10.1021/acs.jpclett.9b02233
L2  - https://pubs.acs.org/doi/10.1021/acs.jpclett.9b02233
N2  - Nuclear magnetic relaxation provides invaluable quantitative site specific information on the dynamics of complex systems. Determining dynamics on nanosecond time scales requires relaxation measurements at low magnetic fields incompatible with high-resolution NMR. Here, we use a two-field NMR spectrometer to measure carbon-13 transverse and longitudinal relaxation rates at a field as low as 0.33 T (proton Larmor frequency 14 MHz) in specifically labeled side chains of the protein ubiquitin. The use of radiofrequency pulses enhances the accuracy of measurements as compared to high-resolution relaxometry approaches, where the sample is moved in the stray field of the superconducting magnet. Importantly, we demonstrate that accurate measurements at a single low magnetic field provide enough information to characterize complex motions on low nanosecond time scales, which opens a new window for the determination of site-specific nanosecond motions in complex systems such as proteins.
ER  -

KADEŘÁVEK, Pavel, N. BOLIK-COULON, S.F. COUSIN, T. MARQUARDSEN, J.M. TYBURN, J.N. DUMEZ and F. FERRAGE. Protein Dynamics from Accurate Low-Field Site-Specific Longitudinal and Transverse Nuclear Spin Relaxation. \textit{Journal of Physical Chemistry Letters}. Washington: American Chemical Society, 2019, vol.~10, No~19, p.~5917-5922. ISSN~1948-7185. Available from: https://dx.doi.org/10.1021/acs.jpclett.9b02233.

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