Rare events and increasing opportunities: Towards combatting amyloid disease
Understanding how different proteins assemble into the ordered, insoluble aggregates associated with amyloid disease is a formidable challenge. Whilst it is generally accepted that protein misfolding is required for the formation of amyloid fibrils, the point at which the folding and aggregation free energy landscapes diverge, and the role of different amino acid residues in determining folding versus aggregation, remain obscure. Even more challenging is the identification of early aggregation-prone monomers and oligomeric species and their structural characterisation, since such species are aggregation-prone, short-lived and rapidly equilibrating. In this lecture I will describe how different biophysical methods are being used to reveal the mechanism by which normally soluble proteins convert into amyloidogenic conformations, how bimolecular collisions between protein variants can result in very different outcomes of assembly and how we have used small molecules to modulate the aggregation process.
Date:
11 March 2016, 11:00 (Friday, 8th week, Hilary 2016)
Venue:
Wellcome Trust Centre for Human Genetics, Headington OX3 7BN
Venue Details:
Meeting Rooms A & B
Speaker:
Prof Sheena Radford (Astbury Centre for Structural Molecular Biology, University of Leeds)
Organising department:
Wellcome Trust Centre for Human Genetics
Organiser:
Eleanor Martin (Wellcome Trust Centre for Human Genetics)
Organiser contact email address:
jones-pa@strubi.ox.ac.uk
Hosts:
Prof E.Yvonne Jones (University of Oxford),
Prof David Stuart (University of Oxford)
Part of:
Strubi seminars
Booking required?:
Not required
Audience:
Members of the University only
Editors:
Eleanor Martin,
Agata Krupa
