NEMPSIA

"Neutrons for Membrane Protein Structure, Interactions, and Assembly"

 Coordinatore INSTITUT MAX VON LAUE - PAUL LANGEVIN 

 Organization address address: 6 Rue Jules Horowitz
city: GRENOBLE
postcode: 38000

contact info
Titolo: Prof.
Nome: Trevor
Cognome: Forsyth
Email: send email
Telefono: +33 4 76207158

 Nazionalità Coordinatore France [FR]
 Totale costo 83˙885 €
 EC contributo 83˙885 €
 Programma FP7-PEOPLE
Specific programme "People" implementing the Seventh Framework Programme of the European Community for research, technological development and demonstration activities (2007 to 2013)
 Code Call FP7-PEOPLE-2011-IIF
 Funding Scheme MC-IIF
 Anno di inizio 2012
 Periodo (anno-mese-giorno) 2012-03-01   -   2013-02-28

 Partecipanti

# participant  country  role  EC contrib. [€] 
1    INSTITUT MAX VON LAUE - PAUL LANGEVIN

 Organization address address: 6 Rue Jules Horowitz
city: GRENOBLE
postcode: 38000

contact info
Titolo: Prof.
Nome: Trevor
Cognome: Forsyth
Email: send email
Telefono: +33 4 76207158

FR (GRENOBLE) coordinator 83˙885.70

Mappa


 Word cloud

Esplora la "nuvola delle parole (Word Cloud) per avere un'idea di massima del progetto.

lipids    bacteriophage    structure    straus    scattering    lipopeptides    group    area    membrane       proteins    team    nuclear    interaction    small    lipid    sans    structural    neutron    magnetic    angle    filamentous    france    resonance   

 Obiettivo del progetto (Objective)

'Understanding membrane protein structure, interaction between these proteins and lipids, and how membrane proteins assemble in the membrane are as of yet unsolved problems of structural biology. This proposal aims to further our understanding in these areas by uniquely combining structural and biophysical data obtained from nuclear magnetic resonance experiments (Straus` area of expertise) with neutron methods, such as small angle neutron scattering (SANS), reflectometry, and neutron diffraction (Forsyth`s and other ILL members` area of research). Specifically, the team will focus their attention on three areas: 1) membrane perturbing antibiotic structure; 2) interaction of lipopeptides with the essential bacterial cell wall biosynthesis component lipid II; and 3) the assembly of membrane proteins in lipids, as studied using the tractable system of B5 filamentous bacteriophage. The proposed projects will not only enable Straus to expand her repertoire in structural methods by exposing her to a host of neutron methodology, but will also cement a strong partnership between Canada and France. The projects will also involve the close collaboration of a number of research groups in France and Germany: the group of Michel Gauthier in Nantes, a leading expert in B5 filamentous bacteriophage and the group of Hans-Georg Sahl in Bonn, who have worked extensively on characterizing interactions between lipopeptides and lipid II. The interdisciplinary nature of the proposed work and the strength of the team will ensure success on all fronts.'

Introduzione (Teaser)

Membrane proteins are important biomolecules whose structure and function are still largely a mystery. EU-funded researchers used techniques like solid-state nuclear magnetic resonance (NMR) and small-angle neutron scattering (SANS) to resolve this.

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