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SUMMARY:Chaperone-guided protein folding at the single-molecule level - Pr
 of. Sander Tans\, Delft University of Technology\, The Netherlands
DTSTART:20140606T110000Z
DTEND:20140606T120000Z
UID:TALK52816@talks.cam.ac.uk
CONTACT:Dr. Judith B. Rommel
DESCRIPTION:Chaperones have been speculated to affect the protein conforma
 tional search for their native state. We address this issue by manipulatin
 g single protein chains using optical tweezers. We found that the chaperon
 e Trigger Factor binds folded structures smaller than one domain\, which a
 re then stable for seconds and ultimately convert to the native state. Tri
 gger Factor stimulates native folding by suppressing misfolding interactio
 ns between domains in constructs of repeated MBP domains. The results indi
 cate that Trigger Factor promotes correct folding by protecting partially 
 folded states from interactions that produce stable misfolded states. As T
 rigger Factor interacts with most newly-synthesized proteins in Escherichi
 a coli\, these findings may be of general importance in understanding prot
 ein folding pathways.
LOCATION:Unilever Lecture Theatre\, Department of Chemistry
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