Multiple valence electron detachment following Auger decay of inner-shell vacancies in gas-phase DNA

Autor: Markus Gühr, Dennis Mayer, Wen Li, Xin Wang, O. Kavatsyuk, Wessel Douma, Michal Ryszka, Ronnie Hoekstra, Matthew S. Robinson, Jean-Christophe Poully, Thomas Schlathölter, Marwa Abdelmouleh, Mathieu Lalande

Publikováno v: Chemical Science
Chemical Science, 12(39), 13177-13186. ROYAL SOC CHEMISTRY
Chemical science 12(39), 13177-13186 (2021). doi:10.1039/D1SC02885E
Chemical Science, The Royal Society of Chemistry, In press, ⟨10.1039/D1SC02885E⟩
Chemical Science, In press, ⟨10.1039/D1SC02885E⟩

We have studied soft X-ray photoabsorption in the doubly deprotonated gas-phase oligonucleotide [dTGGGGT–2H]2−. The dominating decay mechanism of the X-ray induced inner shell vacancy was found to be Auger decay with detachment of at least three

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::833b90da2e9c45a3ba85e5a3d1259af0
http://europepmc.org/articles/PMC8513815

Investigation of the carbon monoxide dication lifetime using (CO)2 dimer fragmentation

Autor: S. Guillous, A. Méry, Amine Cassimi, Wania Wolff, Xavier Flechard, V. Kumar, Mathieu Lalande, Jimmy Rangama

Publikováno v: Physical Review A
Physical Review A, American Physical Society 2021, 104 (4), pp.042813. ⟨10.1103/PhysRevA.104.042813⟩
Physical Review A, 2021, 104 (4), pp.042813. ⟨10.1103/PhysRevA.104.042813⟩

The fragmentation of carbon monoxide dimers induced by collisions with low energy Ar$^{9+}$ ions is investigated using the COLTRIMS technique. The presence of a neighbor molecule in the dimer serves here as a diagnostic tool to probe the lifetimes of

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0e1aedb5582a9daaf76a42cffd6a2eed
https://hal.archives-ouvertes.fr/hal-03313237

Mass Spectral Signatures of Complex Post-Translational Modifications in Proteins: A Proof-of-Principle Based on X-ray Irradiated Vancomycin

Autor: Jean-Christophe Poully, Marwa Abdelmouleh, Samuel Eden, Thomas Schlathölter, Andre Rebelo, Johnny El Feghaly, Violaine Vizcaino, Mathieu Lalande

Publikováno v: Journal of the American Society for Mass Spectrometry, 31(8), 1738-1743. SPRINGER
Journal of The American Society for Mass Spectrometry
Journal of The American Society for Mass Spectrometry, Springer Verlag (Germany), 2020, 31 (8), pp.1738-1743. ⟨10.1021/jasms.0c00169⟩
Journal of The American Society for Mass Spectrometry, 2020, 31 (8), pp.1738-1743. ⟨10.1021/jasms.0c00169⟩

International audience; Characterizing post-translational modifications (PTM) of proteins is of key relevance for the understanding of many biological processes, as these covalent modifications strongly influence or even determine protein function. A

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ae36ab5dfa652254f42b4071314763da
https://research.rug.nl/en/publications/2edbc6ea-dee8-4a58-a988-68add734eee7

Isolated Collagen Mimetic Peptide Assemblies Have Stable Triple-Helix Structures

Autor: Clothilde Comby-Zerbino, Mathilde Bouakil, Fabien Chirot, Jean-Christophe Poully, Mathieu Lalande, Philippe Dugourd

Publikováno v: Chemistry-A European Journal
Chemistry-A European Journal, Wiley-VCH Verlag, 2018, 24 (52), pp.13728-13733. ⟨10.1002/chem.201802929⟩
Chemistry-A European Journal, 2018, 24 (52), pp.13728-13733. ⟨10.1002/chem.201802929⟩

International audience; The origin of the triple-helix structure and high stability of collagen has been debated for many years. As models of the triple helix and building blocks for new biomaterials, collagen mimetic peptide (CMP) assemblies have be

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::54887ec18a84a17591fe1038bcf3c445
https://doi.org/10.1002/chem.201802929

Direct Radiation Effects on the Structure and Stability of Collagen and Other Proteins

Autor: Jean-Christophe Poully, Thomas Schlathölter, Lucas Schwob, Mathieu Lalande, Fabien Chirot, Violaine Vizcaino, Philippe Dugourd

Publikováno v: ChemBioChem 20(24), 2972-2980 (2019). doi:10.1002/cbic.201900202
ChemBioChem, 20(24), 2972-2980. WILEY-V C H VERLAG GMBH
ChemBioChem
ChemBioChem, 2019, 20, pp.1-10. ⟨10.1002/cbic.201900202⟩
ChemBioChem, Wiley-VCH Verlag, 2019, 20, pp.1-10. ⟨10.1002/cbic.201900202⟩

International audience; In this review, recent progress in understanding the direct effects of radiation on the structure and stability of collagen, the most abundant protein in the human body, and other proteins is surveyed. Special emphasis is plac

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::42b2e997e5f7f32a9b7af49e3e0bbea6
https://bib-pubdb1.desy.de/record/434731