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SUMMARY:Molecular Chaperone Functions in Protein Folding and Quality Contr
 ol - Ulrich Hartl\, max Planck Institute of Biochemistry
DTSTART:20161115T120000Z
DTEND:20161115T120000Z
UID:TALK68189@talks.cam.ac.uk
CONTACT:Scientific Meetings Co-ordinator
DESCRIPTION:The past two decades have witnessed a paradigm shift in our un
 derstanding of cellular protein folding. While the three-dimensional struc
 tures of functional proteins are determined by their amino acid sequences\
 , it is now firmly established that in the cell many proteins depend on mo
 lecular chaperones to reach their folded states efficiently and on a biolo
 gically relevant time scale. Assistance of protein folding is provided by 
 different types of chaperone which act to prevent misfolding and aggregati
 on\, often in an ATP-dependent mechanism. Molecular chaperones also cooper
 ate with the degradation machinery (ubiquitin-proteasome system and autoph
 agy) in the removal of terminally misfolded proteins. \n\nOnce folded\, ma
 ny proteins continue to require chaperones to retain their functional stat
 es\, especially under conditions of cell stress. Failure of the chaperone 
 network to maintain proteostasis\, i.e. the conformational integrity of th
 e cellular proteome\, facilitates the manifestation of diseases in which p
 roteins misfold and are deposited as aggregates\, such as Parkinsons and H
 untingtons disease. Proteostasis undergoes a decline during aging\, presum
 ably explaining why age is a major risk factor of neurodegenerative pathol
 ogies.
LOCATION:Max Perutz Lecture Theatre\, Medical Research Council (MRC) (MRC 
 Laboratory of Molecular Biol
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