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SUMMARY:Protein dynamics and amyloid formation: two sides of the same coin
  - Alfonso de Simone (University of Cambridge)
DTSTART:20091016T130000Z
DTEND:20091016T140000Z
UID:TALK20209@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 systemic amyloido
 ses. Besides their feared pathological nature\, amyloids represent an appe
 aling target for many research disciplines including Material Science\, Bi
 otechnology and Chemistry. The seminar will focus on two amyloidogenic sys
 tems. In the case of class I hydrophobins\, the self-assembly into polymer
 s sharing large similarities with amyloids is functional and allows for th
 e formation of water-repellent monolayers on the surface of structures suc
 h as spores and fruiting bodies. In the case of acylphosphatase\, specific
  conditions promote an accidental aggregation into amyloids via mechanisms
  typical of the processes occurring in vivo at the insurgence of amyloid d
 iseases.\nCombined approaches of experiments and multiscale simulations ha
 ve been employed to point out the intimate connection between protein dyna
 mics and self-assembly. The data will show how subtle variations in the co
 nformational free energy of protein monomers govern the processes leading 
 to amyloid formation.
LOCATION:Small Lecture Theatre\, Cavendish Laboratory
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