Coordinatore | CONSORZIO INTERUNIVERSITARIO RISONANZE MAGNETICHE DI METALLOPROTEINE PARAMAGNETICHE
Organization address
address: Via Luigi Sacconi 6 contact info |
Nazionalità Coordinatore | Italy [IT] |
Totale costo | 3˙431˙831 € |
EC contributo | 3˙431˙831 € |
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-2010-ITN |
Funding Scheme | MC-ITN |
Anno di inizio | 2010 |
Periodo (anno-mese-giorno) | 2010-11-01 - 2014-10-31 |
# | ||||
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1 |
CONSORZIO INTERUNIVERSITARIO RISONANZE MAGNETICHE DI METALLOPROTEINE PARAMAGNETICHE
Organization address
address: Via Luigi Sacconi 6 contact info |
IT (SESTO FIORENTINO) | coordinator | 580˙132.94 |
2 |
THE CHANCELLOR, MASTERS AND SCHOLARS OF THE UNIVERSITY OF CAMBRIDGE
Organization address
address: The Old Schools, Trinity Lane contact info |
UK (CAMBRIDGE) | participant | 561˙771.20 |
3 |
CENTRE NATIONAL DE LA RECHERCHE SCIENTIFIQUE
Organization address
address: Rue Michel -Ange 3 contact info |
FR (PARIS) | participant | 529˙875.94 |
4 |
EUROPEAN MOLECULAR BIOLOGY LABORATORY
Organization address
address: Meyerhofstrasse 1 contact info |
DE (HEIDELBERG) | participant | 477˙452.03 |
5 |
VIB
Organization address
address: Rijvisschestraat 120 contact info |
BE (ZWIJNAARDE - GENT) | participant | 469˙476.34 |
6 |
BIOTALENTUM TUDASFEJLESZTO KFT
Organization address
address: AULICH LAJOS UTCA 26 contact info |
HU (GOEDOELLO) | participant | 331˙464.30 |
7 |
GIOTTO BIOTECH SRL
Organization address
address: VIA MADONNA DEL PIANO 6 contact info |
IT (SESTO FIORENTINO FI) | participant | 258˙621.83 |
8 |
Bruker Biospin AG
Organization address
address: Industriestrasse 26 contact info |
CH (Faellanden) | participant | 223˙037.40 |
9 |
MAGYAR TUDOMANYOS AKADEMIA SZEGEDI BIOLOGIAI KOZPONT ENZIMOLOGIAI INTEZET
Organization address
address: Karolina ut 29-31 contact info |
HU (BUDAPEST) | participant | 0.00 |
10 |
PROTERA SRL
Organization address
address: Viale delle Idee 22 contact info |
IT (Sesto Fiorentino (FI)) | participant | 0.00 |
Esplora la "nuvola delle parole (Word Cloud) per avere un'idea di massima del progetto.
'Recent evidence shows that a large share of proteins gain functional advantages by remaining natively unstructured, either completely or partially, thus challenging well-established concepts in structural biology. In order to characterize the highly dynamical nature of such “intrinsically disordered proteins”, and follow their (possible) reorganization by interacting with partners, new integrated multidisciplinary approaches combining a variety of experimental and computational techniques are needed. Our proposal is focused on NMR spectroscopy, since this technique offers an arsenal of effective tools for the study of the structural and dynamical properties of disordered states of proteins at atomic resolution in systems as complex as whole cells. In order to achieve the full potential of this approach, however, current methods should be further developed and properly interfaced with other complementary techniques. The purpose of our network is thus to establish a framework to train a new generation of young researchers and help them develop the necessary skills to successfully respond to the challenges associated with the elucidation of the functional role of intrinsically disordered protein states. If achieved, this goal will provide us with a more quantitative understanding of the biochemical processes at the basis of life and have a significant impact in biomedical research and in the design of new drugs.'
Proteins take on a variety of shapes to carry out different functions that are vital for all living organisms. Unlike commonly accepted structural biology concepts, recent evidence indicates that most proteins remain to some extent in unstructured form to achieve such functionality
Five top-notch institutes in biomedical research partnered under the EU-funded project 'High resolution tools to understand the functional role of protein intrinsic disorder' (http://www.idpbynmr.eu/home/ (IDPBYNMR)) to elucidate the functional role of such intrinsically disordered proteins (IDPs). Nuclear magnetic resonance (NMR) is the core method to provide atomic scale resolution for protein characterisation after developing suitable methods and complementary techniques.
Newly recruited PhD students worked on challenging research projects to obtain potentially useful experimental data for determining the structure-function relationship of IDPs. Several intensive training courses were also conducted, involving by the major experts in the fields, to provide multidisciplinary expertise.
IDPBYNMR researchers have developed new computational techniques and NMR methods for studies on IDPs in cellular systems. Viral IDPs associated with hijacking cell regulation and amyloids linked to several diseases were successfully characterised. The scientists have designed and completed the http://pedb.vib.be/ (database) for IDP and experimental data.
Project activities could be the key to developing new educational and training programs for this relatively new field of IDPs. Potential applications are numerous particularly in the biomedical and pharmaceutical sector. This could lead to the development of novel and effective drug candidates and biomarkers to detect, treat and monitor treatment progress in patients.