PHYSPROT

Determining Physical Properties of Heterogeneous Protein Complexes in Small Volumes

Coordinatore	THE CHANCELLOR, MASTERS AND SCHOLARS OF THE UNIVERSITY OF CAMBRIDGE    more Spiacenti, non ci sono informazioni su questo coordinatore. Contattare Fabio per maggiori infomrazioni, grazie.
Nazionalità Coordinatore	United Kingdom [UK]
Totale costo	1˙499˙895 €
EC contributo	1˙499˙895 €
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-2013-StG
Funding Scheme	ERC-SG
Anno di inizio	2014
Periodo (anno-mese-giorno)	2014-02-01   -   2019-01-31

 Partecipanti

#	participant	country	role	EC contrib. [€]
1	THE CHANCELLOR, MASTERS AND SCHOLARS OF THE UNIVERSITY OF CAMBRIDGE  Organization address address: The Old Schools, Trinity Lane city: CAMBRIDGE postcode: CB2 1TN contact info Titolo: Dr. Nome: Tuomas Pertti Jonathan Cognome: Knowles Email: send email Telefono: +44 1223 760313 Fax: +44 1223 336362	UK (CAMBRIDGE)	hostInstitution	1˙499˙895.00
2	THE CHANCELLOR, MASTERS AND SCHOLARS OF THE UNIVERSITY OF CAMBRIDGE  Organization address address: The Old Schools, Trinity Lane city: CAMBRIDGE postcode: CB2 1TN contact info Titolo: Ms. Nome: Renata Cognome: Schaeffer Email: send email Telefono: +44 1223 333543 Fax: +44 1223 332988	UK (CAMBRIDGE)	hostInstitution	1˙499˙895.00

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 Obiettivo del progetto (Objective)

'The objective of this proposal is to probe in aqueous solution protein complexes which are both heterogeneous and possess highly variable stoichiometries. The study of heterogeneous protein systems by conventional means is very challenging since most current biophysical methods perform best for pure solutions of isolated components - yet proteins exert in the majority of cases their biological functionality through forming complexes. We propose in this application that the key to study such systems is to operate in much smaller volumes than in conventional biophysical experiments. We will use microfluidics to obtain information about the physical properties of protein complexes in real time through quantitative micron-scale measurements of mass transport of molecular species under the action of diffusion and electric or centrifugal fields. Furthermore, by working in small volumes, we will study nucleation phenomena inherent to many protein self-assembly phenomena on the level of single nucleation events by segregating individual nuclei into spatially distinct compartments. Modern microfabrication techniques that allow for the manipulation of liquids on the picolitre scales required for this project are available and will be exploited, but the potential of this technology to define experimentally highly heterogeneous protein complexes in terms of their key fundamental physical properties, such as the hydrodynamic radius, charge and mass, and shed light on the physical basis of protein self-assembly, have remained unexploited. Using this approach, we will explore biological problems of fundamental and practical importance characterised by heterogeneity, including functional chaperone complexes, formation and detection of amyloid oligomers and studies of complex biomolecular mixtures. This programme will deliver fundamentally new approaches to study heterogeneous protein complexes and will shed light on the physical principles that govern protein self-assembly.'