Zobrazeno 1 - 10
of 89
pro vyhledávání: '"Fabien, Ferrage"'
Autor:
K. Ivanov, John Blanchard, Dmitry Budker, Fabien Ferrage, Alexey Kiryutin, Tobias Sjolander, Alexandra Yurkovskaya, Ivan Zhukov
Publikováno v:
Two‐Dimensional (2D) NMR Methods. :395-414
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::9770eb5ebbe3293ffa766084b9cf5f4f
https://doi.org/10.1002/9781119806721.ch13
https://doi.org/10.1002/9781119806721.ch13
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
Publikováno v:
Molecules, Vol 20, Iss 12, Pp 21992-21999 (2015)
The proper characterization of protein-ligand interfaces is essential for structural biology, with implications ranging from the fundamental understanding of biological processes to pharmacology. Nuclear magnetic resonance is a powerful technique for
Externí odkaz:
https://doaj.org/article/9395bef62f534db1a438a4ee8bee87c8
Autor:
Nicola, Salvi, Vojtěch, Zapletal, Zuzana, Jaseňáková, Milan, Zachrdla, Petr, Padrta, Subhash, Narasimhan, Thorsten, Marquardsen, Jean-Max, Tyburn, Lukáš, Žídek, Martin, Blackledge, Fabien, Ferrage, Pavel, Kadeřávek
Publikováno v:
Biophysical Journal
Biophysical Journal, 2022, 121 (20), pp.3785-3794. ⟨10.1016/j.bpj.2022.09.016⟩
Biophysical Journal, 2022, 121 (20), pp.3785-3794. ⟨10.1016/j.bpj.2022.09.016⟩
International audience; Intrinsically disordered proteins (IDPs) or intrinsically disordered regions (IDRs) is a class of biologically important proteins exhibiting specific biophysical characteristics. They lack a hydrophobic core, and their conform
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e5898807fff2dd8639a7294778ef9a36
https://hal.science/hal-03861375/file/Salvi_BJ_text_preaccepted_4FF.pdf
https://hal.science/hal-03861375/file/Salvi_BJ_text_preaccepted_4FF.pdf
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
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d5efeb234ecfca0cf1f913e5075f073e
https://doi.org/10.1007/s10858-021-00361-1
https://doi.org/10.1007/s10858-021-00361-1
Autor:
Olof Stenström, Candide Champion, Marc Lehner, Guillaume Bouvignies, Sereina Riniker, Fabien Ferrage
Publikováno v:
Current Opinion in Structural Biology
Current Opinion in Structural Biology, 2022, 77, pp.102459. ⟨10.1016/j.sbi.2022.102459⟩
Current Opinion in Structural Biology, 77
Current Opinion in Structural Biology, 2022, 77, pp.102459. ⟨10.1016/j.sbi.2022.102459⟩
Current Opinion in Structural Biology, 77
Nuclear magnetic resonance (NMR) spin relaxation experi-ments currently probe molecular motions on timescales from picoseconds to nanoseconds. The detailed interpretation of these motions in atomic detail benefits from complementarity with the result
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7d7a10cdbd495ec9f4b78767fb809eaf
https://pubmed.ncbi.nlm.nih.gov/36148743
https://pubmed.ncbi.nlm.nih.gov/36148743
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