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SUMMARY:Conformational Conversion  in Amyloid Assembly - Sheena Radford\, 
 University of Leeds
DTSTART:20131003T151500Z
DTEND:20131003T170000Z
UID:TALK44710@talks.cam.ac.uk
CONTACT:Scientific Meetings Co-ordinator
DESCRIPTION:Understanding how different proteins assemble into the ordered
 \, insoluble aggregates associated with amyloid disease is a formidable ch
 allenge. Whilst it is generally accepted that protein unfolding is require
 d for the formation of amyloid fibrils from natively folded proteins in vi
 tro and\, therefore\, presumably also in vivo\, the point at which the fol
 ding and aggregation free energy landscapes diverge\, and the role of diff
 erent amino acid residues in determining folding versus aggregation\, rema
 in obscure. Even more challenging is the identification of early oligomeri
 c species and their structural characterisation\, since such species are a
 ggregation-prone\, short-lived and rapidly equilibrating.  Using an array 
 of different biophysical methods and approaches\, I will describe our rece
 nt experiments which have used NMR paramagnetic relaxation experiments\, a
 longside other biophysical methods\, to reveal the mechanism by which conf
 ormational conversion of the normally soluble protein\, beta-2-microglobul
 in into an amyloidogenic conformation occurs and how bimolecular collision
 s between protein variants can result in very different outcomes of assemb
 ly. The insights gained may help to derive new routes to the modulation of
  aggregation and lead to fascinating questions about the cooperativity of 
 protein structures and how this modulates their behaviours in assembly. 
LOCATION:Max Perutz Lecture Theatre\, Medical Research Council (MRC) (MRC 
 Laboratory of Molecular Biol
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