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SUMMARY:Switching to the dark side: Repositioning of Polyglutamine Repeat 
 Promotes Amyloid Fibril Formation by the Model Protein\, β-Lactamase BlaP
  - Dr Mireille Dumoulin\, University of Liege
DTSTART:20170503T093000Z
DTEND:20170503T103000Z
UID:TALK72422@talks.cam.ac.uk
CONTACT:23027
DESCRIPTION:The abnormal expansion of polyglutamine (polyQ) tracts above a
  threshold length within proteins is associated with an increased propensi
 ty of the protein to aggregate into amyloid fibrils. Such expansions in ni
 ne human proteins lead to nine distinct neurodegenerative amyloidoses. Whi
 le repeat length and aggregation are well correlated\, the non-polyQ regio
 ns of these proteins can also play a very significant role\, both preventa
 tive and facilitative\, in the aggregation process. We engineered chimeric
  proteins via the insertion of polyQ repeats of various lengths at differe
 nt locations of a model protein scaffold\, the β-lactamase BlaP and we in
 vestigate the impact of polyQ position on the structure\, stability\, and 
 aggregation propensity of the enzyme. The results of these experiments hig
 hlight the environment-sensitivity of polyQ protein aggregation\, particul
 arly with regards to the stability/dynamics of the host protein and to the
  properties of sequences flanking the polyQ tract\, and contribute to a be
 tter understanding of how the overall protein context modulates the amyloi
 d fibril-forming propensity of polyQ-containing proteins.
LOCATION:Department of Chemistry\, Cambridge\, Unilever lecture theatre
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