FORCEMAP
Intramolecular force mapping of enzymes in action: the role of strain in motor mechanisms
| Coordinatore | EOTVOS LORAND TUDOMANYEGYETEM
Spiacenti, non ci sono informazioni su questo coordinatore. Contattare Fabio per maggiori infomrazioni, grazie. |
| Nazionalità Coordinatore | Hungary [HU] |
| Totale costo | 750˙000 € |
| EC contributo | 750˙000 € |
| 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-2007-StG |
| Funding Scheme | ERC-SG |
| Anno di inizio | 2008 |
| Periodo (anno-mese-giorno) | 2008-09-01 - 2014-08-31 |
Partecipanti
| # | ||||
|---|---|---|---|---|
| 1 |
EOTVOS LORAND TUDOMANYEGYETEM
Organization address
address: EGYETEM TER 1-3 contact info |
HU (BUDAPEST) | hostInstitution | 0.00 |
| 2 |
EOTVOS LORAND TUDOMANYEGYETEM
Organization address
address: EGYETEM TER 1-3 contact info |
HU (BUDAPEST) | hostInstitution | 0.00 |
Mappa
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Obiettivo del progetto (Objective)
'A fundamental but unexplored problem in biology is whether and how enzymes use mechanical strain during their functioning. It is now evident that the knowledge of atomic structures and chemical interactions is not sufficient to understand the intricate mechanisms underlying enzyme specificity and efficiency. Several lines of evidence suggest that mechanical effects play crucial roles in enzyme activity. Therefore we aim to create detailed force maps that reveal how the intramolecular distribution of mechanical strains changes during the enzyme cycle and how these rearrangements drive the enzyme processes. The applicability of current nanotechniques for the investigation of this problem is limited because they do not allow simultaneous measurement of mechanical and enzymatic parameters. Thus we seek to open new avenues of research by developing site-specific sensors and passive or photoinducible molecular springs to measure force-dependent chemical/structural changes with high spatiotemporal resolution in myosin. Since force perturbations occur very rapidly, we are able to combine experimental studies with quasi-realistic in silico simulations to describe the physical background of enzyme function. We expect that our research will yield fundamental insights into the role of intramolecular strains in enzymes and thus greatly aid the design and control of enzyme processes (specificity, activity, regulation). Our studies may also lead to new paradigms in the understanding of motor systems.'