Convergent vews on disordered protein dynamics from NMR and computational approaches

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⟩

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

Quantum Chemical Calculations of NMR Chemical Shifts in Phosphorylated Intrinsically Disordered Proteins

Autor: Jana Pavlíková Přecechtělová, Jozef Hritz, Vojtěch Zapletal, Arnošt Mládek

Publikováno v: Journal of Chemical Theory and Computation. 15:5642-5658

Quantum mechanics (QM) calculations are applied to examine 1H, 13C, 15N, and 31P chemical shifts of two phosphorylation sites in an intrinsically disordered protein region. The QM calculations employ a combination of (1) structural ensembles generate

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fc64359cb9309f4013b5331e93d7c0c5
https://doi.org/10.1021/acs.jctc.8b00257

Boosting the resolution of low-field 15 N relaxation experiments on intrinsically disordered proteins with triple-resonance NMR

Autor: Jean-Max Tyburn, Vojtěch Zapletal, Milan Zachrdla, Nicolas Bolik-Coulon, Pavel Kadeřávek, Petr Padrta, Zuzana Jaseňáková, Thorsten Marquardsen, Fabien Ferrage, Lukáš Žídek

Publikováno v: Journal of Biomolecular NMR
Journal of Biomolecular NMR, 2020, 74 (2-3), pp.139-145. ⟨10.1007/s10858-019-00298-6⟩
Journal of Biomolecular NMR, Springer Verlag, 2020, 74 (2-3), pp.139-145. ⟨10.1007/s10858-019-00298-6⟩

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 re

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::90dcc5a617604f244d5912c64a7b4cde
https://doi.org/10.1007/s10858-019-00298-6

Structure and functions of microtubule associated proteins tau and MAP2c: Similarities and differences

Autor: Malene Ringkjøbing Jensen, Rostislav Skrabana, Subhash Narasimhan, Kateřina Melková, Lukáš Žídek, Markus Zweckstetter, Vojtěch Zapletal, Martin Blackledge, Jozef Hritz, Séverine Jansen

Publikováno v: Biomolecules
Biomolecules, MDPI, 2019, 9 (3), pp.105. ⟨10.3390/biom9030105⟩
Biomolecules 9(3), 105 (2019). doi:10.3390/biom9030105
Biomolecules, 2019, 9 (3), pp.105. ⟨10.3390/biom9030105⟩
Biomolecules, Vol 9, Iss 3, p 105 (2019)

The stability and dynamics of cytoskeleton in brain nerve cells are regulated by microtubule associated proteins (MAPs), tau and MAP2. Both proteins are intrinsically disordered and involved in multiple molecular interactions important for normal phy

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::73ce6f56ea1f06603272c2b4a1083981
https://hdl.handle.net/21.11116/0000-0003-3553-421.11116/0000-0003-3555-221.11116/0000-0003-3556-1

Functionally specific binding regions of microtubule-associated protein 2c exhibit distinct conformations and dynamics

Autor: Martin Blackledge, Jozef Hritz, Vojtěch Zapletal, Séverine Jansen, Markus Zweckstetter, Malene Ringkjøbing Jensen, Jiří Nováček, Kateřina Melková, Erik Nomilner, Milan Zachrdla, Lukáš Žídek

Publikováno v: Journal of Biological Chemistry
Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2018, 293 (34), pp.13297-13309. ⟨10.1074/jbc.RA118.001769⟩
Journal of Biological Chemistry, 2018, 293 (34), pp.13297-13309. ⟨10.1074/jbc.RA118.001769⟩
The journal of biological chemistry 293(34), 13297-13309 (2018). doi:10.1074/jbc.RA118.001769

International audience; Microtubule-associated protein 2c (MAP2c) is a 49-kDa intrinsically disordered protein regulating the dynamics of microtubules in developing neurons. MAP2c differs from its sequence homologue Tau in the pattern and kinetics of

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::09391220f8952424f9ba98cc0852a23a
https://hal.archives-ouvertes.fr/hal-01995909