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© Sandrine Etienne-Manneville
Photo prise à l'avant (dans la protrusion) d'astrocytes primaires de rat en migration. Marquage par immunofluorescence montrant en rouge, p150 Glued, une protéine associée aux extrémités 'plus' des microtubules et en vert la tubuline des microtubules. La photographie montre l'accumulation de p150 Glued à l'avant des cellules en migration, où la protéine pourrait participer à l'ancrage des microtubules à la membrane plasmique. Pour essayer de corriger, les dérèglements observés lors de la migration des cellules d'astrocytes tumuraux ou gliomes on cherche à connaitre les mécanismes moléculaires fondamentaux qui controlent la polarisation et la migration cellulaires.
Publication : Journal of the American Chemical Society

Side chain resonances in static oriented proton-decoupled 15N solid-state NMR spectra of membrane proteins

Scientific Fields
Diseases
Organisms
Applications
Technique

Published in Journal of the American Chemical Society - 13 May 2009

Aisenbrey C, Prongidi-Fix L, Chenal A, Gillet D, Bechinger B

Link to Pubmed [PMID] – 19374351

J. Am. Chem. Soc. 2009 May;131(18):6340-1

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 labeling not only of the backbone amides but also of nitrogens localized within the side chains of arginine, glutamine, tryptophan, asparagines, lysines, and histidines. Most of these side chain resonances appear in the spectral region of the anisotropic backbone amides, and residual intensities have been observed also in cross-polarization spectra. In the past this issue has received little attention although it can cause ambiguities during assignment. Here we show that by combining cross-polarization and Hahn echo solid-state NMR experiments, it is possible to differentiate between side chain and backbone resonances. This is demonstrated using experimental and simulated (15)N spectra of oriented purple membranes, diphtheria toxin T domain and Bcl-x(L).

https://www.ncbi.nlm.nih.gov/pubmed/19374351