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SUMMARY:The hydrophobic effect characterises the thermodynamic signature o
 f amyloid fibril growth - Dr Sanne Abeln\, Vrije University Amsterdam
DTSTART:20201125T143000Z
DTEND:20201125T153000Z
UID:TALK150124@talks.cam.ac.uk
CONTACT:Lisa Masters
DESCRIPTION:Most proteins fold in the cell into stable\, compact structure
 s. Nevertheless\, many proteins also have the ability to stick together\, 
 forming long fibrillar structures that are associated with a wide range of
  human disorders including Alzheimer’s and Parkinson’s disease. The ex
 act nature of the amyloid-causing stickiness is not well understood\, neve
 rtheless amyloid fibrils show some very specific thermodynamic characteris
 tics. Some fibrils even destabilise at low temperatures. In this work we t
 ranslate hydrophobic theory previously used to model protein folding to fi
 bril formation. We combine this theory with experimental measurements\, si
 mulations and meta-data analysis and we consider several different types o
 f fibrils. This allows us to unravel the nature of the stickiness in amylo
 id fibrils. Overall\, we show that amyloid fibril elongation is associated
  with a negative heat capacity\, the magnitude of which correlates closely
  with the hydrophobic surface area that is buried upon fibril formation\, 
 highlighting the importance of hydrophobicity for fibril stability.\n
LOCATION:Zoom - link to be announced
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