Time-Resolved Protein Side-Chain Motions Unraveled by
High-Resolution Relaxometry and Molecular Dynamics Simulations

J 2018

Time-Resolved Protein Side-Chain Motions Unraveled by High-Resolution Relaxometry and Molecular Dynamics Simulations

COUSIN, S.F.; Pavel KADEŘÁVEK; N. BOLIK-COULON; Y. GU; C. CHARLIER et al.

Základní údaje

Originální název

Time-Resolved Protein Side-Chain Motions Unraveled by High-Resolution Relaxometry and Molecular Dynamics Simulations

Autoři

COUSIN, S.F.; Pavel KADEŘÁVEK ; N. BOLIK-COULON; Y. GU; C. CHARLIER; L. GARBER; L. BRUSCHWEILER-LI; T. MARQUARDSEN; J.M. TYBURN; R. BRUSCHWEILER a F. FERRAGE

Vydání

Journal of the American Chemical Society, Washington, American Chemical Society, 2018, 0002-7863

Další údaje

Jazyk

angličtina

Typ výsledku

Článek v odborném periodiku

Obor

10402 Inorganic and nuclear chemistry

Stát vydavatele

Spojené státy

Utajení

není předmětem státního či obchodního tajemství

Odkazy

URL

Impakt faktor

Impact factor: 14.695

Označené pro přenos do RIV

Ano

Kód RIV

RIV/00216224:14740/18:00104556

Organizační jednotka

Středoevropský technologický institut

Klíčová slova anglicky

NUCLEAR MAGNETIC-RELAXATION; ORDER-PARAMETER ANALYSIS; C-13 NMR-SPECTROSCOPY; DEUTERIUM SPIN PROBES; METHYL-GROUP DYNAMICS; MODEL-FREE APPROACH; AMBER FORCE-FIELDS; SOLID-STATE NMR; CONFORMATIONAL ENTROPY; BACKBONE PARAMETERS

Štítky

rivok

Příznaky

Mezinárodní význam, Recenzováno

Změněno: 13. 3. 2019 11:35, Mgr. Pavla Foltynová, Ph.D.

Anotace

V originále

Motions of proteins are essential for the performance of their functions. Aliphatic protein side chains and their motions play critical roles in protein interactions: for recognition and binding of partner molecules at the surface or serving as an entropy reservoir within the hydrophobic core. Here, we present a new NMR method based on high-resolution relaxometry and high-field relaxation to determine quantitatively both motional amplitudes and time scales of methyl-bearing side chains in the picosecond-to-nanosecond range. We detect a wide variety of motions in isoleucine side chains in the protein ubiquitin. We unambiguously identify slow motions in the low nanosecond range, which, in conjunction with molecular dynamics computer simulations, could be assigned to transitions between rotamers. Our approach provides unmatched detailed insight into the motions of aliphatic side chains in proteins and provides a better understanding of the nature and functional role of protein side-chain motions.

Citovat

COUSIN, S.F.; Pavel KADEŘÁVEK; N. BOLIK-COULON; Y. GU; C. CHARLIER; L. GARBER; L. BRUSCHWEILER-LI; T. MARQUARDSEN; J.M. TYBURN; R. BRUSCHWEILER a F. FERRAGE. Time-Resolved Protein Side-Chain Motions Unraveled by High-Resolution Relaxometry and Molecular Dynamics Simulations. Journal of the American Chemical Society. Washington: American Chemical Society, 2018, roč. 140, č. 41, s. 13456-13465. ISSN 0002-7863. Dostupné z: https://doi.org/10.1021/jacs.8b09107.

@article{1470464,
   author = {Cousin, S.F. and Kadeřávek, Pavel and BolikandCoulon, N. and Gu, Y. and Charlier, C. and Garber, L. and BruschweilerandLi, L. and Marquardsen, T. and Tyburn, J.M. and Bruschweiler, R. and Ferrage, F.},
   article_location = {Washington},
   article_number = {41},
   doi = {https://doi.org/10.1021/jacs.8b09107},
   keywords = {NUCLEAR MAGNETIC-RELAXATION; ORDER-PARAMETER ANALYSIS; C-13 NMR-SPECTROSCOPY; DEUTERIUM SPIN PROBES; METHYL-GROUP DYNAMICS; MODEL-FREE APPROACH; AMBER FORCE-FIELDS; SOLID-STATE NMR; CONFORMATIONAL ENTROPY; BACKBONE PARAMETERS},
   language = {eng},
   issn = {0002-7863},
   journal = {Journal of the American Chemical Society},
   title = {Time-Resolved Protein Side-Chain Motions Unraveled by High-Resolution Relaxometry and Molecular Dynamics Simulations},
   url = {https://pubs.acs.org/doi/10.1021/jacs.8b09107},
   volume = {140},
   year = {2018}
}

TY  - JOUR
ID  - 1470464
AU  - Cousin, S.F. - Kadeřávek, Pavel - Bolik-Coulon, N. - Gu, Y. - Charlier, C. - Garber, L. - Bruschweiler-Li, L. - Marquardsen, T. - Tyburn, J.M. - Bruschweiler, R. - Ferrage, F.
PY  - 2018
TI  - Time-Resolved Protein Side-Chain Motions Unraveled by High-Resolution Relaxometry and Molecular Dynamics Simulations
JF  - Journal of the American Chemical Society
VL  - 140
IS  - 41
SP  - 13456-13465
EP  - 13456-13465
PB  - American Chemical Society
SN  - 00027863
KW  - NUCLEAR MAGNETIC-RELAXATION
KW  - ORDER-PARAMETER ANALYSIS
KW  - C-13 NMR-SPECTROSCOPY
KW  - DEUTERIUM SPIN PROBES
KW  - METHYL-GROUP DYNAMICS
KW  - MODEL-FREE APPROACH
KW  - AMBER FORCE-FIELDS
KW  - SOLID-STATE NMR
KW  - CONFORMATIONAL ENTROPY
KW  - BACKBONE PARAMETERS
UR  - https://pubs.acs.org/doi/10.1021/jacs.8b09107
N2  - Motions of proteins are essential for the performance of their functions. Aliphatic protein side chains and their motions play critical roles in protein interactions: for recognition and binding of partner molecules at the surface or serving as an entropy reservoir within the hydrophobic core. Here, we present a new NMR method based on high-resolution relaxometry and high-field relaxation to determine quantitatively both motional amplitudes and time scales of methyl-bearing side chains in the picosecond-to-nanosecond range. We detect a wide variety of motions in isoleucine side chains in the protein ubiquitin. We unambiguously identify slow motions in the low nanosecond range, which, in conjunction with molecular dynamics computer simulations, could be assigned to transitions between rotamers. Our approach provides unmatched detailed insight into the motions of aliphatic side chains in proteins and provides a better understanding of the nature and functional role of protein side-chain motions.
ER  -

COUSIN, S.F.; Pavel KADEŘÁVEK; N. BOLIK-COULON; Y. GU; C. CHARLIER; L. GARBER; L. BRUSCHWEILER-LI; T. MARQUARDSEN; J.M. TYBURN; R. BRUSCHWEILER a F. FERRAGE. Time-Resolved Protein Side-Chain Motions Unraveled by High-Resolution Relaxometry and Molecular Dynamics Simulations. \textit{Journal of the American Chemical Society}. Washington: American Chemical Society, 2018, roč.~140, č.~41, s.~13456-13465. ISSN~0002-7863. Dostupné z: https://doi.org/10.1021/jacs.8b09107.

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