BIOMEMOS
Higher order structure and function of biomembranes
| Coordinatore | AARHUS UNIVERSITET
Spiacenti, non ci sono informazioni su questo coordinatore. Contattare Fabio per maggiori infomrazioni, grazie. |
| Nazionalità Coordinatore | Denmark [DK] |
| Totale costo | 2˙444˙180 € |
| EC contributo | 2˙444˙180 € |
| Programma | FP7-IDEAS-ERC
Specific programme: "Ideas" implementing the Seventh Framework Programme of the European Community for research, technological development and demonstration activities (2007 to 2013) |
| Code Call | ERC-2009-AdG |
| Funding Scheme | ERC-AG |
| Anno di inizio | 2010 |
| Periodo (anno-mese-giorno) | 2010-04-01 - 2015-03-31 |
Partecipanti
| # | ||||
|---|---|---|---|---|
| 1 |
AARHUS UNIVERSITET
Organization address
address: Nordre Ringgade 1 contact info |
DK (AARHUS C) | hostInstitution | 2˙444˙180.00 |
| 2 |
AARHUS UNIVERSITET
Organization address
address: Nordre Ringgade 1 contact info |
DK (AARHUS C) | hostInstitution | 2˙444˙180.00 |
Mappa
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Obiettivo del progetto (Objective)
'The biomembrane is a prerequisite of life. It enables the cell to maintain a controlled environment and to establish electrochemical gradients as rapidly accessible energy stores. Biomembranes also provide scaffold for organisation and spatial definition of signal transmission in the cell. Crystal structures of membrane proteins are determined with an increasing pace. Along with functional studies integral studies of individual membrane proteins are now widely implemented. The BIOMEMOS proposal goes a step further and approaches the function of the biomembrane at the higher level of membrane protein complexes. Through a combination of X-ray crystallography, electrophysiology, general biochemistry, biophysics and bioinformatics and including also the application of single-particle cryo-EM and small-angle X-ray scattering, the structure and function of membrane protein complexes of key importance in life will be investigated. The specific targets for investigation in this proposal include: 1) higher-order complexes of P-type ATPase pumps such as signalling complexes of Na,K-ATPase, and 2) development of methods for structural studies of membrane protein complexes Based on my unique track record in structural studies of large, difficult structures (ribosomes and membrane proteins) in the setting of a thriving research community in structural biology and biomembrane research in Aarhus provides a critical momentum for a long-term activity. The activity will take advantage of the new possibilities offered by synchrotron sources in Europe. Furthermore, a single-particle cryo-EM research group formed on my initiative in Aarhus, and a well-established small-angle X-ray scattering community provides for an optimal setting through multiple cues in structural biology and functional studies'