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Protein dynamics and misfolding: the case study of a multidomain protein related to an amyloid disease

Obiettivo

The present proposal aims to study the relationships existing between protein structural dynamics and pathological aggregation of the multidomain N-terminal part of the polyglutamine (polyQ) protein ataxin-3. By means of an integrated approach combining advanced NMR and computational techniques, the applicant plans to investigate low frequencies native-like states responsible of aberrant protein-protein interactions leading to first amyloid aggregates. These species in AT3 predominantly involve the globular structured N-terminal domain and are polyQ independent. Results of this project will boost the knowledge related to the first misfolding events leading to AT3 pathological aggregation as well as our understanding on subtle misfolding events triggering protein aggregation of folded globular proteins.

Invito a presentare proposte

FP7-PEOPLE-2012-IEF
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Coordinatore

KOBENHAVNS UNIVERSITET
Contributo UE
€ 230 809,80
Indirizzo
NORREGADE 10
1165 Kobenhavn
Danimarca

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Regione
Danmark Hovedstaden Byen København
Tipo di attività
Higher or Secondary Education Establishments
Contatto amministrativo
Ivan Kristoffersen (Mr.)
Collegamenti
Costo totale
Nessun dato