B2LiVe, a label-free 1D-NMR method to quantify the binding of amphitropic peptides or proteins to membrane vesicles

Autor: Mirko Sadi, Nicolas Carvalho, Corentin Léger, Bruno Vitorge, Daniel Ladant, J. Iñaki Guijarro, Alexandre Chenal

Publikováno v: Cell Reports: Methods, Vol 3, Iss 11, Pp 100624- (2023)

Summary: Amphitropic proteins and peptides reversibly partition from solution to membrane, a key process that regulates their functions. Experimental approaches classically used to measure protein partitioning into lipid bilayers, such as fluorescenc

Externí odkaz: https://doaj.org/article/98dbe9fa67214533aca3fb57a878a923

B2LiVe, a label-free 1D-NMR method to quantify the binding of amphitropic peptides or proteins to membrane vesicles

Autor: Mirko Sadi, Nicolas Carvalho, Bruno Vitorge, Daniel Ladant, J. Iñaki Guijarro, Alexandre Chenal

SummaryAmphitropic proteins and peptides reversibly partition from solution to membrane, a key process that regulates their functions. Experimental approaches, such as fluorescence and circular dichroism, are classically used to measure the partition

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4cf4f3d0e052a90148c514e58d2dcd7f
https://doi.org/10.1101/2022.12.14.520471

1H, 15N and 13C resonance assignments and secondary structure of PulG, the major pseudopilin from Klebsiella oxytoca type 2 secretion system

Autor: Bruno Vitorge, Aracelys López-Castilla, Nelly Morellet, Nadia Izadi-Pruneyre, Léa Khoury, Olivera Francetic

Publikováno v: Biomolecular NMR Assignments
Biomolecular NMR Assignments, 2017, 11 (2), pp.155-158. ⟨10.1007/s12104-017-9738-7⟩
Biomolecular NMR Assignments, Springer, 2017, 11 (2), pp.155-158. ⟨10.1007/s12104-017-9738-7⟩

International audience; Bacteria use complex transporters to secrete functionally relevant proteins to the extracellular medium. The type 2 secretion system (T2SS) translocates folded proteins involved in bacterial nutrient acquisition, virulence and

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::37e2c78dbc94f47d75731b753c0e10df
https://hal.science/hal-02326254

Spectral Aliasing: A Super Zoom for 2D-NMR Spectra. Principles and Applications

Autor: Philippe Christen, Jean-Marc Nuzillard, Gaétan Bayiha Ba Njock, Bruno Vitorge, Dieudonné Emmanuel Pegnyemb, Damien Jeannerat, Trixie Ann Bartholomeusz, Mohamadali Foroozandeh, Rupali Shivapurkar

Publikováno v: CHIMIA, Vol 64, Iss 4 (2010)
Chimia, Vol. 64, No 4 (2010) pp. 235-240

The NMR methodology based on spectral aliasing developed at the University of Geneva is reviewed. Different approaches aimed at increasing the resolution in the indirect carbon dimension of 2D heteronuclear experiments are presented with their respec

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f2ae47e04fc941bf0de2077861fe1498
https://www.chimia.ch/chimia/article/view/4839

High-precision heteronuclear 2D NMR experiments using 10-ppm spectral window to resolve carbon overlap

Autor: Bruno Vitorge, Orlando Muñoz, Sandra Loss, Kurt Hostettmann, Munir Humam, Damien Jeannerat, Philippe Christen, Stefan Bieri

Publikováno v: Chemical communications (Cambridge England)
Chemical Communications, No 8 (2009) pp. 950-952

The acquisition of a complementary heteronuclear 2D NMR experiment with 10-ppm carbon window allows chemists to improve by a factor 20–25 the spectral resolution and determine carbon chemical shifts with five figures from 2D spectra.

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b1af19705d4f6422a095b0fe03922b6c
https://doi.org/10.1039/b820478k