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SUMMARY:Probing unfolded and intrinsically disordered proteins with single
 -molecule spectroscopy
DTSTART:20170406T150000
DTEND:20170406T161500
DTSTAMP:20260407T110903Z
UID:050f0d48d32c25fd10fe5c0397759f5b99d58f597005830fdfda4888
CATEGORIES:Conferences - Seminars
DESCRIPTION:Prof. Ben Schuler\, University of Zurich\nThe functions of pro
 teins have traditionally been linked to their well-defined three-dimension
 al\, folded structures. It is becoming increasingly clear\, however\, that
  many proteins perform essential functions without being folded. Single-mo
 lecule spectroscopy provides new opportunities for investigating the struc
 ture and dynamics of such unfolded or ‘intrinsically disordered’ prote
 ins (IDPs). The combination of single-molecule Förster resonance energy t
 ransfer (FRET) with nanosecond correlation spectroscopy\, microfluidic mix
 ing\, and related methods can be used to probe intra- and intermolecular d
 istance distributions\, reconfiguration dynamics\, and interactions on a w
 ide range of timescales\, and even in heterogeneous environments\, includi
 ng live cells.\n 
LOCATION:BCH 2218 https://plan.epfl.ch/?room==BCH%202218
STATUS:CONFIRMED
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