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SUMMARY:Elucidating molecular mechanisms on and off the pathway to amyloid
  deposition - Andrew Miranker
DTSTART:20080130T103000Z
DTEND:20080130T113000Z
UID:TALK9756@talks.cam.ac.uk
CONTACT:Giorgio Favrin
DESCRIPTION:Polypeptide chains have a generic capacity to self-associate i
 nto linear\, non-covalent assemblies termed amyloid fibers.  Such fibers g
 ive the appearance of violating basic principles of protein folding becaus
 e they can serve as templates of their own propagation.  Regardless of the
  identity of the starting precursor\, the resultant amyloid structures sha
 re a number of properties.  These include insolubility\, protease resistan
 ce\, chemical resistance and cytotoxicity.  Proteins are therefore under s
 elective pressure to avoid this phenomenon and are most commonly associate
 d with diseases of advancing age\, such as Alzheimer’s\, and diseases as
 sociated with medical therapy\, such as dialysis related amyloidosis (DRA)
 .  In our laboratory\, we investigate fibrillogenesis as a biologically re
 levant chemical reaction.  Therefore\, understanding the mechanism of asse
 mbly requires insight into the structures\, energetics and pathways which 
 relate different intermediate states.  In general\, insights are elusive d
 ue to the transient and heterogeneous nature of fibrillogenesis.  We are n
 evertheless able to shed light by combining a range of biophysical approac
 hes and focusing on protein systems ranging from peptide models to globula
 r proteins.  The commonality among such investigations reveals the rules g
 overning this class of polymeric assembly.\n
LOCATION:Unilever Lecture Theatre\, Unilever Centre\, Department of Chemis
 try
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