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SUMMARY:The molecular machinery of protein degradation - structural studie
 s ex situ and in situ
DTSTART:20170406T163000
DTEND:20170406T173000
DTSTAMP:20260510T135053Z
UID:b8798a10c420b8796104024c4c5ddadfe9ee98a431acf1eb3a0b4064
CATEGORIES:Conferences - Seminars
DESCRIPTION:Prof. Wolfgang Baumeister\, \nMax Planck Institute of Biochem
 istry\nGermany\n \nThe 26S proteasome operates at the executive end of th
 e ubiquitin-proteasome pathway for the controlled degradation of intracell
 ular proteins. The 2.5 MDa complex is built of 34 different subunits and c
 omprises two subcomplexes: the 20S core where proteolysis takes place and 
 one or two regulating particles which prepare substrates for degradation. 
 Whereas the structure of its 20S core particle has been determined by X-ra
 y crystallography two decades ago\, the structure of the 19S regulatory pa
 rticle\, which recruits substrates\, unfolds them\, and translocates them 
 to the core particle for degradation\, has been determined only in recent 
 years.\n \nCryo electron tomography allows to perform structural studies 
 of macromolecular and supramolecular structures in situ\, i.e. in their fu
 nctional cellular environments. We used this method to study 26S proteasom
 es in a number of cellular settings revealing their precise location\, ass
 embly and activity status as well as their interactions with other parts o
 f the degradation machinery.\n \n 
LOCATION:BCH 2201 https://plan.epfl.ch/?room==BCH%202201
STATUS:CONFIRMED
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