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SUMMARY:Chaperonin-assisted protein folding: &quot\;The peculiar case of t
 he bacteriophage T4 major capsid protein&quot\; - Prof Saskia van der Vies
  (Vrije Universiteit Amsterdam)
DTSTART:20100112T160000Z
DTEND:20100112T170000Z
UID:TALK21948@talks.cam.ac.uk
CONTACT:Dr Mark Miller
DESCRIPTION:The E.coli\, chaperonin machine (GroEL-GroES) is responsible f
 or folding 15% of the newly-synthesized proteins in particular those with 
 complex 3D structures. \nBacteriophages like lambda and T5 utilise the hos
 t's chaperonin machinery for the folding of some of their protein structur
 es. Interestingly bacteriophage T4 \nrequires a hybrid GroEL-gp31 chaperon
 in complex for the folding of the major capsid protein. Although the amino
  acid sequence of gp31 and GroES is only 14% identical the overall structu
 re appears similar. Cryo electron microscopy and image reconstruction of t
 he GroEL-gp31-ADP complex revealed that the folding cavity is slightly lar
 ger than of the GroEL-GroES-ADP complex\, which is consistent with the siz
 e of the capsid protein (56kDa) that is close to the maximum size that is 
 thought to fit inside the folding cage. It is not fully \nunderstood why G
 roES is unable to assist the folding of the T4 capsid protein.  Stuctural 
 and dynamics analysis of the chaperonin-assisted folding of the capsid pro
 tein will be presented and the molecular requirements for folding will be 
 discussed.
LOCATION:Unilever Lecture Theatre\, Department of Chemistry
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