MANIFOLD
"Manipulating folding, assembly and disassembly of protein complexes - from molecule to disease"
| Coordinatore | UNIVERSITEIT UTRECHT
Organization address
address: Heidelberglaan 8 contact info |
| Nazionalità Coordinatore | Netherlands [NL] |
| Totale costo | 2˙633˙837 € |
| EC contributo | 2˙633˙837 € |
| 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-2012-ITN |
| Funding Scheme | MC-ITN |
| Anno di inizio | 2012 |
| Periodo (anno-mese-giorno) | 2012-09-01 - 2016-08-31 |
Partecipanti
| # | ||||
|---|---|---|---|---|
| 1 |
UNIVERSITEIT UTRECHT
Organization address
address: Heidelberglaan 8 contact info |
NL (UTRECHT) | coordinator | 2˙633˙837.50 |
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Obiettivo del progetto (Objective)
'ManiFold is organised by researchers and teachers of the Bijvoet Graduate School for Biomolecular Sciences to achieve 3 key aims: (i) Moving the Bijvoet towards a Graduate School with annual rhythm and specific recruitment moments. (ii) Centering the research around focus areas to stimulate synergies. (iii) Strengthening the links of the School to private enterprises and international partners. ManiFold aims to extend its impact to the entire Bijvoet School by creating a coherent group of selected students that gel around one theme, large enough that we expect the group to have a strong influence, but such that it fits the capacity of our excellent educational programme. The Bijvoet groups have a longstanding track record in structural biology and outstanding expertise in large-scale infrastructure. In ManiFold, we focus our studies on protein folding and misfolding events at various levels, focusing on conceptual advances regarding the folding of newly-synthesized proteins, the assembly and disassembly of protein oligomers and complexes, conformational changes of proteins upon activation or deactivation, allosteric effects, protein misfolding and amyloid formation, the activity of molecular chaperones on those processes, and the monitoring of protein-protein interactions at the proteome level. The coherent class of students working on this multidisciplinary theme will allow us create synergisms and increase the quality of our education. From the joint effort on this topic we expect a lasting impact on training in our Bijvoet School, our international position and on the links of our School with the private sector.'