PROTEIN DYNAMICS

Conformational dynamics of proteins in the solid state

 Coordinatore ECOLE NORMALE SUPERIEURE DE LYON 

 Organization address address: 46 Allee d'Italie
city: LYON
postcode: 69364

contact info
Titolo: Ms.
Nome: Valérie
Cognome: Tessier
Email: send email
Telefono: +33 4 72 72 80 00
Fax: +33 4 72 72 80 80

 Nazionalità Coordinatore France [FR]
 Totale costo 0 €
 EC contributo 176˙803 €
 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-IEF-2008
 Funding Scheme MC-IEF
 Anno di inizio 2009
 Periodo (anno-mese-giorno) 2009-11-01   -   2011-10-31

 Partecipanti

# participant  country  role  EC contrib. [€] 
1    ECOLE NORMALE SUPERIEURE DE LYON

 Organization address address: 46 Allee d'Italie
city: LYON
postcode: 69364

contact info
Titolo: Ms.
Nome: Valérie
Cognome: Tessier
Email: send email
Telefono: +33 4 72 72 80 00
Fax: +33 4 72 72 80 80

FR (LYON) coordinator 176˙803.80

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malfunction    proteins    consistent    time    transitions    protein    dynamics    dynamic    data    solid    molecular    motions    nmr    conformational    plays   

 Obiettivo del progetto (Objective)

'Conformational dynamics are intimately linked to the biological activity of proteins, thereby regulating the essential processes of life. In particular protein motion plays an essential role in catalysis, allowing conformational rearrangements to align key catalytic amino acids and in ligand binding allowing the entry of co-factors into areas that would otherwise be inaccessible. Mobility also plays a major role in the thermodynamic stability of functional states; in molecular recognition processes that often involve disorder-to-order transitions; and in allostery and molecular signalling, where correlated molecular motions can transmit information between distant sites in a protein. Dynamic transitions also mediate the onset of pathological malfunction and disease. NMR spectroscopy is uniquely suited to study a large number of these dynamic processes, resolving detailed and important site-specific information about motions spanning a vast range of time scales in both folded and unfolded proteins, and in both the liquid and the solid phase. We believe that the key to understanding the complex relationship between protein dynamics and molecular function and malfunction requires an accurate description of the behavior of proteins in their different phases and forms, and an understanding of the transition between different states. In this study we are interested in developing a self-consistent framework for measuring and describing protein dynamics in the solid state. To this end in this project we propose to develop a number of NMR methods extending substantially the scope of accessible protein motions in solids. This work is a part of concerted collaborative effort that couples for the first time NMR data from both solid and solutions with complementary data from elastic incoherent neutron scattering and molecular simulation in order to provide a general consistent picture of dynamical processes in proteins.'

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