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SUMMARY:Protein dynamics and amyloid formation: two sides of the same coin
  - Alfonso de Simone (University of Cambridge)
DTSTART:20090918T130000Z
DTEND:20090918T140000Z
UID:TALK20150@talks.cam.ac.uk
CONTACT:Erika Eiser
DESCRIPTION:One of the most intriguing issues in biology is the occasional
  conversion of proteins from their folded functional forms into thread-lik
 e molecular aggregates designated as amyloids. These transformations into 
 an alternative form of protein structure are linked to over 40 pathologica
 l conditions ranging from neurodegenerative disorders to\nsystemic amyloid
 oses. Besides their feared pathological nature\, amyloids represent an app
 ealing target for many research disciplines including Material Science\,Bi
 otechnology and Chemistry.\n\nThe seminar will focus on two amyloidogenic 
 systems. In the case of class I hydrophobins\, the self-assembly into poly
 mers sharing large similarities with amyloids is functional and allows for
  the formation of water-repellent monolayers on\nthe surface of structures
  such as spores and fruiting bodies. In the case of acylphosphatase\, spec
 ific conditions promote an accidental aggregation into amyloids via mechan
 isms typical of the processes occurring in vivo at the insurgence of amylo
 id diseases.\n\nCombined approaches of experiments and multiscale simulati
 ons have been employed to point out the intimate connection between protei
 n dynamics and self-assembly. The data will show how subtle variations in 
 the conformational free energy of protein monomers govern the processes le
 ading to amyloid formation.
LOCATION:Small Lecture Theatre\, Cavendish Laboratory
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