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PROTEIN DYNAMICS

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Conformational dynamics of proteins in the solid state

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 r... ver más

31/10/2011

ENS LYON

177K€

Presupuesto del proyecto: 177K€

Líder del proyecto

ECOLE NORMALE SUPERIEURE DE LYON No se ha especificado una descripción o un objeto social para esta compañía.

Fecha límite participación Sin fecha límite de participación.

Financiación concedida El organismo FP7 notifico la concesión del proyecto el día 2011-10-31 No tenemos la información de la convocatoria

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1 Participantes

ENS LYON

176.80K€ | Lider

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Líder del proyecto

ECOLE NORMALE SUPERIEURE DE LYON No se ha especificado una descripción o un objeto social para esta compañía.

Presupuesto del proyecto 177K€

Fecha límite de participación Sin fecha límite de participación.

Descripción del proyecto 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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