Zobrazeno 1 - 10
of 25
pro vyhledávání: '"Nicolas Bolik-Coulon"'
Publikováno v:
Nature Communications, Vol 14, Iss 1, Pp 1-12 (2023)
Protein phosphatase 1 (PP1) is regulated by intrinsically disordered proteins like inhibitor-3, I3. The authors show that I3 does not inhibit PP1 by forming a rigid complex but instead by binding dynamically with its active site metals, showing how f
Externí odkaz:
https://doaj.org/article/bc1b46cd9ddd4042aaeae3d56346b97c
Publikováno v:
Journal of Magnetic Resonance Open, Vol 4, Iss , Pp 100007- (2020)
Biomolecular NMR spectroscopy has greatly benefited from the development of TROSY-type pulse sequences, in pair with specific labeling. The selection of spin operators with favorable relaxation properties has led to an increase in the resolution and
Externí odkaz:
https://doaj.org/article/7189b92a60b745f88f55c54a3b9101d9
Autor:
Nicolas Bolik-Coulon, Milan Zachrdla, Guillaume Bouvignies, Philippe Pelupessy, Fabien Ferrage
Relaxometry consists in measuring relaxation rates over orders of magnitude of magnetic fields to probe motions of complex systems. High-resolution relaxometry (HRR) experiments can be performed on conventional high-field NMR magnets equipped with a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::72ef2f5164f4449e4a8c7c62cf98dcba
https://doi.org/10.26434/chemrxiv-2023-b8qn6
https://doi.org/10.26434/chemrxiv-2023-b8qn6
Autor:
Tae Hun Kim, Michael L. Nosella, Nicolas Bolik-Coulon, Robert W. Harkness, Shuya Kate Huang, Lewis E. Kay
Publikováno v:
Proceedings of the National Academy of Sciences. 120
Epigenetic modifications of chromatin play a critical role in regulating the fidelity of the genetic code and in controlling the translation of genetic information into the protein components of the cell. One key posttranslational modification is ace
Autor:
Nicolas Bolik-Coulon, Alexander I.M. Sever, Robert W. Harkness, James M. Aramini, Yuki Toyama, D. Flemming Hansen, Lewis E. Kay
Publikováno v:
Journal of magnetic resonance (San Diego, Calif. : 1997). 346
The HMQC pulse sequence and variants thereof have been exploited in studies of high molecular weight protein complexes, taking advantage of the fact that fast and slow relaxing magnetization components are sequestered along two distinct magnetization
Publikováno v:
Journal of biomolecular NMR. 76(5-6)
For the past decade chemical exchange saturation transfer (CEST) experiments have been successfully applied to study exchange processes in biomolecules involving sparsely populated, transiently formed conformers. Initial implementations focused on ex
Publikováno v:
Journal of Biomolecular NMR
Journal of Biomolecular NMR, 75 (2-3)
Journal of Biomolecular NMR, Springer Verlag, 2021, ⟨10.1007/s10858-021-00361-1⟩
Journal of Biomolecular Nmr
Journal of Biomolecular NMR, 75 (2-3)
Journal of Biomolecular NMR, Springer Verlag, 2021, ⟨10.1007/s10858-021-00361-1⟩
Journal of Biomolecular Nmr
The dynamics of molecules in solution is usually quantified by the determination of timescale-specific amplitudes of motions. High-resolution nuclear magnetic resonance (NMR) relaxometry experiments—where the sample is transferred to low fields for
Autor:
Nicolas Bolik-Coulon, Olivier Languin-Cattoën, Diego Carnevale, Milan Zachrdla, Damien Laage, Fabio Sterpone, Guillaume Stirnemann, Fabien Ferrage
Publikováno v:
Physical Review Letters
Physical Review Letters, 2022, 129 (20), pp.203001. ⟨10.1103/PhysRevLett.129.203001⟩
Physical Review Letters, 2022, 129 (20), pp.203001. ⟨10.1103/PhysRevLett.129.203001⟩
International audience; Nuclear magnetic relaxation is widely used to probe protein dynamics. For decades, most analyses of relaxation in proteins have relied successfully on the model-free approach, forgoing mechanistic descriptions of motions. Mode
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::860bef531d5d3dbacc1ac41f601adf08
http://arxiv.org/abs/2204.05813
http://arxiv.org/abs/2204.05813
Autor:
Nicolas Bolik-Coulon, Fabien Ferrage
Nuclear Magnetic Resonance (NMR) is a tool of choice to characterize molecular motions. In biological macromolecules, pico- to nanosecond motions, in particular, can be probed by nuclear spin relaxation rates, which depend on the time fluctuations of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e7fa819b1861a43c9dff5d3a542443ed
Autor:
Jean-Nicolas Dumez, Jean-Max Tyburn, Samuel F. Cousin, Fabien Ferrage, Pavel Kadeřávek, Nicolas Bolik-Coulon, Thorsten Marquardsen
Publikováno v:
Journal of Physical Chemistry Letters
Journal of Physical Chemistry Letters, American Chemical Society, 2019, 10 (19), pp.5917-5922. ⟨10.1021/acs.jpclett.9b02233⟩
Journal of Physical Chemistry Letters, 2019, 10 (19), pp.5917-5922. ⟨10.1021/acs.jpclett.9b02233⟩
Journal of Physical Chemistry Letters, American Chemical Society, 2019, 10 (19), pp.5917-5922. ⟨10.1021/acs.jpclett.9b02233⟩
Journal of Physical Chemistry Letters, 2019, 10 (19), pp.5917-5922. ⟨10.1021/acs.jpclett.9b02233⟩
International audience; Nuclear magnetic relaxation provides invaluable quantitative site-specific information on the dynamics of complex systems. Determining dynamics on nanosecond timescales requires relaxation measurements at low magnetic fields,