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Understanding protein misfolding and aggregation by NMR

Understanding protein misfolding and aggregation by NMR

Objective

A detailed understanding of the processes responsible for the failure in achieving or in maintaining the normal functional structures of proteins is of crucial importance in the development of strategies to protect or enhance human health. To gain biologic al function, polypeptide chains generally need to fold into specific three- dimensional structures - their native states. Abberrant folding of proteins can lead to a range of other scenarios, including the development of highly organised and intractable ag gregates that are deposited inside or outside cells. Such misfolding events are at the origins of a range of neurological and systemic diseases that increasingly compromise the quality and expectancy of life and the health resources of advanced societies. The focus of this application is the development of novel methods to study the structural slates of proteins that are particularly relevant to understand protein misfolding and aggregation. The species involved range from highly flexible unfolded monomers to soluble oligomers and precursors of fibrillar aggregates. In most of these states, polypeptide chains acquire structures that differ substantially from those of the native proteins that are accessible from conventional approaches of structural biology o r from structural genomics procedures. The major techniques that will be used to define at atomic level the structural characteristics of the range of species relevant to understanding misfolding and aggregation is NMR spectroscopy. In this STREP, a range of complementary NMR approaches will be developed by the various partners for this purpose. These approaches include a variety of NMR techniques and will be coupled with novel computational approaches able to define even the disorganised ensembles characte risitic of some of the most interesting and biologically relevant species. These approaches will then be applied to representative examples of the various types of proteins #

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Coordinator

JOHANN WOLFGANG GOETHE-UNIVERSITAET

Address

Senckenberganlage 31
Frankfurt/Main

Germany

Administrative Contact

Harald SCHWALBE (Prof.)

Participants (8)

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CONSORZIO INTERUNIVERSITARIO RISONANZE MAGNETICHE DI METALLOPROTEINE PARAMAGNETICHE

Italy

UNIVERSITEIT UTRECHT

Netherlands

THE CHANCELLOR, MASTERS AND SCHOLARS OF THE UNIVERSITY OF CAMBRIDGE

United Kingdom

STOCKHOLMS UNIVERSITET

Sweden

KOBENHAVNS UNIVERSITET

Denmark

NATIONAL INSTITUTE OF CHEMICAL PHYSICS AND BIOPHYSICS

Estonia

ZYENTIA LIMITED

United Kingdom

EIDGENÖSSISCHE TECHNISCHE HOCHSCHULE ZUERICH

Switzerland

Project information

Grant agreement ID: 512052

  • Start date

    1 November 2004

  • End date

    30 April 2008

Funded under:

FP6-LIFESCIHEALTH

  • Overall budget:

    € 2 030 000

  • EU contribution

    € 1 900 000

Coordinated by:

JOHANN WOLFGANG GOETHE-UNIVERSITAET

Germany