Zobrazeno 1 - 10
of 22
pro vyhledávání: '"MESH: Nitrogen Isotopes"'
Publikováno v:
Journal of Biomolecular NMR
Journal of Biomolecular NMR, 2018, 72 (3-4), pp.115-124. ⟨10.1007/s10858-018-0216-z⟩
Journal of Biomolecular NMR, Springer Verlag, 2018, 72 (3-4), pp.115-124. ⟨10.1007/s10858-018-0216-z⟩
Journal of Biomolecular NMR, 2018, 72 (3-4), pp.115-124. ⟨10.1007/s10858-018-0216-z⟩
Journal of Biomolecular NMR, Springer Verlag, 2018, 72 (3-4), pp.115-124. ⟨10.1007/s10858-018-0216-z⟩
International audience; Aromatic amino-acid side chains are essential components for the structure and function of proteins. We present herein a set of NMR experiments for time-efficient resonance assignment of histidine and tyrosine side chains in u
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b0b7c57f709ae90d2d777a21bd05b950
https://hal.science/hal-02085961
https://hal.science/hal-02085961
Autor:
Mattia Sturlese, Monica Stefani, Massimo Bellanda, Frank Löhr, Bruno Manta, Marcelo A. Comini, Stefano Mammi
Publikováno v:
Biomolecular NMR Assignments
Biomolecular NMR Assignments, Springer, 2016, 10 (1), pp.85-8. 〈10.1007/s12104-015-9643-x〉
Biomolecular NMR Assignments, Springer, 2016, 10 (1), pp.85-8. 〈10.1007/s12104-015-9643-x〉
International audience; Trypanosomatids are parasites responsible for several tropical and subtropical diseases, such as Chaga's disease, sleeping sickness and Leishmaniasis. In contrast to the mammalian host, the thiol-redox metabolism of these path
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9e6a7a6189af82b20e30cad6182fd350
https://hal-riip.archives-ouvertes.fr/pasteur-01501052
https://hal-riip.archives-ouvertes.fr/pasteur-01501052
Publikováno v:
Biomolecular NMR Assignments
Biomolecular NMR Assignments, 2015, 9 (2), pp.397-401. ⟨10.1007/s12104-015-9617-z⟩
Biomolecular NMR Assignments, Springer, 2015, 9 (2), pp.397-401. ⟨10.1007/s12104-015-9617-z⟩
Biomolecular NMR Assignments, 2015, 9 (2), pp.397-401. ⟨10.1007/s12104-015-9617-z⟩
Biomolecular NMR Assignments, Springer, 2015, 9 (2), pp.397-401. ⟨10.1007/s12104-015-9617-z⟩
The general stress response in Enterobacteria, like Escherichia coli or Salmonella, is controlled by the transcription factor σS, encoded by the rpoS gene, which accumulates during stationary phase growth and associates with the core RNA polymerase
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::898ac162edfdaa003afee48bbdbe959a
https://hal-pasteur.archives-ouvertes.fr/pasteur-01413051/document
https://hal-pasteur.archives-ouvertes.fr/pasteur-01413051/document
Publikováno v:
Biopolymers / Biopolymers (Biospectroscopy); Biopolymers (Pept Sci ); Biopolymers (Peptide Sci ); Biopolymers (Pept Sci); Biopolymers
Biopolymers / Biopolymers (Biospectroscopy); Biopolymers (Pept Sci ); Biopolymers (Peptide Sci ); Biopolymers (Pept Sci); Biopolymers, 2005, 79 (3), pp.139-49. ⟨10.1002/bip.20343⟩
Biopolymers / Biopolymers (Biospectroscopy); Biopolymers (Pept Sci ); Biopolymers (Peptide Sci ); Biopolymers (Pept Sci); Biopolymers, 2005, 79 (3), pp.139-49. ⟨10.1002/bip.20343⟩
Under iron-deficient conditions, the Gram-negative bacterium Pseudomonas aeruginosa ATCC 15692 secretes a peptidic siderophore, pyoverdin PaA, composed of an aromatic chromophore derived from 2,3-diamino-6,7-dihydroxyquinoline and a partially cyclize
Autor:
Nicolas Doucet, Sophie M. C. Gobeil, Joelle N. Pelletier, Jaeok Park, Donald Gagné, Christopher M. Clouthier, Albert M. Berghuis
Publikováno v:
Chemistry and Biology
Chemistry and Biology, Elsevier, 2014, 21 (10), pp.1330-1340. ⟨10.1016/j.chembiol.2014.07.016⟩
Chemistry and Biology, Elsevier, 2014, 21 (10), pp.1330-1340. ⟨10.1016/j.chembiol.2014.07.016⟩
International audience; Proteins are dynamic systems, and understanding dynamics is critical for fully understanding protein function. Therefore, the question of whether laboratory engineering has an impact on protein dynamics is of general interest.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1ba5f695813acb7fee43b56e99069663
https://hal.archives-ouvertes.fr/hal-01196413
https://hal.archives-ouvertes.fr/hal-01196413
Publikováno v:
Chemosphere
Chemosphere, Elsevier, 2007, 69 (4), pp.636-643. ⟨10.1016/j.chemosphere.2007.02.069⟩
Chemosphere, Elsevier, 2007, 69 (4), pp.636-643. 〈10.1016/j.chemosphere.2007.02.069〉
Chemosphere, Elsevier, 2007, 69 (4), pp.636-643. ⟨10.1016/j.chemosphere.2007.02.069⟩
Chemosphere, Elsevier, 2007, 69 (4), pp.636-643. 〈10.1016/j.chemosphere.2007.02.069〉
8 pages; International audience; In a sandy agricultural soil of south-west of France, continuously cultivated with maize and amended with sewage-sludge over 20 years, the behavior of three trace metals (Cu, Pb, and Zn) was studied during the sludge
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f10b0b5c25f62372c16e3f48ab790d75
https://hal.archives-ouvertes.fr/hal-00292924
https://hal.archives-ouvertes.fr/hal-00292924
Autor:
Pascale Tsan, Marc Quinternet, Marie-Christine Averlant-Petit, Guy Branlant, Manh-Thong Cung, Christophe Jacob, Chrystel Beaufils, Sandrine Boschi-Muller, Laure Selme
Publikováno v:
Biomolecular NMR Assignments
Biomolecular NMR Assignments, Springer, 2008, 2 (1), pp.85-7. ⟨10.1007/s12104-008-9091-y⟩
Biomolecular NMR Assignments, Springer, 2008, 2 (1), pp.85-7. ⟨10.1007/s12104-008-9091-y⟩
International audience; We report the nearly complete 1H, 13C, and 15N resonance assignments of the C103S mutant of the N-terminal domain of DsbD from Neisseria meningitides. Secondary structure determination using CSI method leads to the prediction
Autor:
Lydia Prongidi-Fix, Burkhard Bechinger, Alexandre Chenal, Christopher Aisenbrey, Daniel Gillet
Publikováno v:
Journal of the American Chemical Society
Journal of the American Chemical Society, American Chemical Society, 2009, 131 (18), pp.6340-1. ⟨10.1021/ja900677b⟩
Journal of the American Chemical Society, 2009, 131 (18), pp.6340-1. ⟨10.1021/ja900677b⟩
Journal of the American Chemical Society, American Chemical Society, 2009, 131 (18), pp.6340-1. ⟨10.1021/ja900677b⟩
Journal of the American Chemical Society, 2009, 131 (18), pp.6340-1. ⟨10.1021/ja900677b⟩
International audience; Proton-decoupled (15)N solid-state NMR spectra are used to analyze the structure, dynamics, and membrane topology of proteins uniformly labeled with (15)N. Preparation of the proteins by bacterial overexpression results in the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f45179723f3a6edd381e9cc2fe71936c
https://hal-pasteur.archives-ouvertes.fr/pasteur-01509891
https://hal-pasteur.archives-ouvertes.fr/pasteur-01509891
Autor:
Muriel Delepierre, Nicolas Wolff, Christophe Prehaud, Henri Buc, Catherine Simenel, Elouan Terrien, Monique Lafon
Publikováno v:
Biomolecular NMR Assignments
Biomolecular NMR Assignments, Springer, 2009, 3 (1), pp.45-8. ⟨10.1007/s12104-008-9138-0⟩
Biomolecular NMR Assignments, 2009, 3 (1), pp.45-8. ⟨10.1007/s12104-008-9138-0⟩
Biomolecular NMR Assignments, Springer, 2009, 3 (1), pp.45-8. ⟨10.1007/s12104-008-9138-0⟩
Biomolecular NMR Assignments, 2009, 3 (1), pp.45-8. ⟨10.1007/s12104-008-9138-0⟩
International audience; Most of microbes hijack the cellular machinery to their advantage by interacting with specific target of the host cell. Glycoprotein of rabies virus is a key factor controlling the homeostasis of infected neuronal cells and pr
Publikováno v:
Nature Protocols
Nature Protocols, 2008, 3 (2), pp.235-41. ⟨10.1038/nprot.2007.498⟩
Nature Protocols, Nature Publishing Group, 2008, 3 (2), pp.235-41. ⟨10.1038/nprot.2007.498⟩
Nature Protocols, 2008, 3 (2), pp.235-41. ⟨10.1038/nprot.2007.498⟩
Nature Protocols, Nature Publishing Group, 2008, 3 (2), pp.235-41. ⟨10.1038/nprot.2007.498⟩
International audience; A nuclear magnetic resonance (NMR) experiment is described for the direct detection of N-H[...]O=C hydrogen bonds (H-bonds) in 15N and 13C isotope-labeled biomolecules. This quantitative 'long-range' HNCO-COSY (correlation spe
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::489d8bbf644cea1712350428b80569b6
https://hal-pasteur.archives-ouvertes.fr/pasteur-00367115
https://hal-pasteur.archives-ouvertes.fr/pasteur-00367115