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SUMMARY:Untangling the Disaggregation Mechanism of the Hsp100 Protein Mach
 ine ClpB”
DTSTART:20230621T101500
DTSTAMP:20260430T100817Z
UID:f5c3cd62d64f65e9dee2b34a24130b035dbb2dcab2e3c83110725c6c
CATEGORIES:Conferences - Seminars
DESCRIPTION:Dr. Remi Casier (Weizmann Institute of Science\, Rehovot\, Is
 rael)\nProtein disaggregases are nano‐sized machines capable of reversin
 g protein aggregation and are vital for maintaining cell homeostasis. Hsp1
 00 disaggregases\, such as ClpB\, are believed to liberate proteins from a
 ggregates by actively pulling a strand of a substrate into a large central
  pore utilizing the energy of ATP hydrolysis. However\, the mechanism util
 ized by ClpB to convert this energy into mechanical force\, including the
  timescale at which this occurs\, remains uncertain. To address this issue
 \, we use single‐molecule FRET spectroscopy to directly observe the dyna
 mic interactions between ClpB and a model substrate\, casein. The real‐t
 ime monitoring of the efficiency of energy transfer between fluorescently 
 tagged casein and ClpB revealed that\, in the presence of ATP\, casein is 
 fully translocated through the central pore of ClpB on the millisecond tim
 escale.
LOCATION:BSP 234 https://plan.epfl.ch/?room==BSP%20234
STATUS:CONFIRMED
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