MEMCURV
Dynamic control of membrane curvature and its role in membrane protein assembly
| Coordinatore | THE CHANCELLOR, MASTERS AND SCHOLARS OF THE UNIVERSITY OF OXFORD
Organization address
address: University Offices, Wellington Square contact info |
| Nazionalità Coordinatore | United Kingdom [UK] |
| Totale costo | 278˙807 € |
| EC contributo | 278˙807 € |
| 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 | 2013 |
| Periodo (anno-mese-giorno) | 2013-02-01 - 2015-01-31 |
Partecipanti
| # | ||||
|---|---|---|---|---|
| 1 |
THE CHANCELLOR, MASTERS AND SCHOLARS OF THE UNIVERSITY OF OXFORD
Organization address
address: University Offices, Wellington Square contact info |
UK (OXFORD) | coordinator | 278˙807.40 |
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Obiettivo del progetto (Objective)
'Changes in the curvature of the cell membrane play an important role in many important biological processes, including cell division, vesicle trafficking, and neurotransmission. These changes in morphology are not just a passive consequence of other events in the cell, but can also drive the action of other proteins. For example, changes in curvature are thought to affect protein binding, the gating kinetics of ion channels, and to direct the localisation of proteins in vivo.
Although current methods can measure the presence of such interactions, they cannot directly measure real-time changes in membrane curvature or correlate individual protein binding events with changes in curvature. Dr Junhong Lu has a proven track record in Biological Atomic Force Microscopy. We propose to combine his expertise with new synthetic mimics of the cell membrane recently produced in the laboratory of Dr Mark Wallace at Oxford University. This combination of methods will enable us to manipulate and characterize the curvature of the cell membrane, and study its effects on protein function using single-molecule methods.'