Aromatic ring flips in differently packed ubiquitin protein crystals from MAS NMR and MD

Autor: Diego F. Gauto, Olga O. Lebedenko, Lea Marie Becker, Isabel Ayala, Roman Lichtenecker, Nikolai R. Skrynnikov, Paul Schanda

Publikováno v: Journal of Structural Biology: X, Vol 7, Iss , Pp 100079- (2023)

Probing the dynamics of aromatic side chains provides important insights into the behavior of a protein because flips of aromatic rings in a protein’s hydrophobic core report on breathing motion involving a large part of the protein. Inherently inv

Externí odkaz: https://doaj.org/article/7b8066b020234babba7e973e524ded5f

Publisher Correction: Functional control of a 0.5 MDa TET aminopeptidase by a flexible loop revealed by MAS NMR

Autor: Diego F. Gauto, Pavel Macek, Duccio Malinverni, Hugo Fraga, Matteo Paloni, Iva Sučec, Audrey Hessel, Juan Pablo Bustamante, Alessandro Barducci, Paul Schanda

Publikováno v: Nature Communications, Vol 13, Iss 1, Pp 1-1 (2022)

Externí odkaz: https://doaj.org/article/b700f5fa44c44071a611f4bfd200650f

Aromatic Ring Dynamics, Thermal Activation, and Transient Conformations of a 468 kDa Enzyme by Specific 1H–13C Labeling and Fast Magic-Angle Spinning NMR

Autor: Diego F. Gauto, David Gajan, Roman J. Lichtenecker, Alessandro Barducci, Audrey Hessel, Masatsune Kainosho, Paul Schanda, Pavel Macek, Yohei Miyanoiri, Tsutomu Terauchi, Jérôme Boisbouvier, Hugo Pacheco de Freitas Fraga

Publikováno v: Journal of the American Chemical Society. 141:11183-11195

Aromatic residues are located at structurally important sites of many proteins. Probing their interactions and dynamics can provide important functional insight but is challenging in large proteins. Here, we introduce approaches to characterize the d

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::243468560f6302c0b2934a75135d56b1
https://doi.org/10.1021/jacs.9b04219

Conformational sampling of the intrinsically disordered dsRBD-1 domain from Arabidopsis thaliana DCL1

Autor: Lingzi Zhao, Diego F. Gauto, Guillermo Hails, Roberta Crespo, Rodolfo M. Rasia, Florencia C. Mascali, Jin Wang, Irina Paula Suarez

Publikováno v: Physical Chemistry Chemical Physics. 20:11237-11246

DCL1 is the ribonuclease that carries out miRNA biogenesis in plants. Substrate pri-miRNA recognition by DCL1 requires two double stranded RNA binding domains located at the C-terminus of the protein. We have previously shown that the first of these

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e62d208ac2ab94d061dcfaee6fe09f19
https://doi.org/10.1039/c7cp07908g

Mechanism of the allosteric activation of the ClpP protease machinery by substrates and active-site inhibitors

Autor: Audrey Hessel, Katharina Weinhäupl, Adrián Velázquez-Campoy, Christophe Chipot, Cécile Morlot, Paul Schanda, Jan Felix, François Dehez, Olga Abian, Hugo Pacheco de Freitas Fraga, Irina Gutsche, Diego F. Gauto

Publikováno v: Zaguán. Repositorio Digital de la Universidad de Zaragoza
instname
'Science Advances ', vol: 5, pages: eaaw3818-1-eaaw3818-19 (2019)
Science Advances
Science Advances, American Association for the Advancement of Science (AAAS), 2019, 5 (9), pp.eaaw3818. ⟨10.1126/sciadv.aaw3818⟩
SCIENCE ADVANCES
Digital.CSIC. Repositorio Institucional del CSIC
Science Advances, 2019, 5 (9), pp.eaaw3818. ⟨10.1126/sciadv.aaw3818⟩

18 pags., 6 figs., 1 tab. -- Open Access funded by Creative Commons Atribution Licence 4.0
Coordinated conformational transitions in oligomeric enzymatic complexes modulate function in response to substrates and play a crucial role in enzyme inh

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7a1324138b0f4d564dc88daa4ccd2c80