BEGIN:VCALENDAR
VERSION:2.0
PRODID:-//Memento EPFL//
BEGIN:VEVENT
SUMMARY:Bridging scales in the coevolution of interacting proteins
DTSTART:20170516T140000
DTSTAMP:20261005T103049Z
UID:6237fda1f25907eef644ae6c94297527dbf29973dbca5a3d975039f5
CATEGORIES:Conferences - Seminars
DESCRIPTION:Prof . Martin Weigt\, Institut de biologie Paris-Seine\, unive
 rsité Pierre et Marie Curie\nBIOLOGICAL & STATISTICAL PHYSICS SEMINAR\n\n
 Understanding protein−protein interactions (PPI) is central to our under
 standing of almost all complex biological processes. Computational tools e
 xploiting rapidly growing genomic databases to characterize PPI are theref
 ore urgently needed. Such methods should address multiple scales of PPI: (
 i) Between two interacting proteins\, which residues are in contact across
  the interfaces? (ii) Inside a genome\, which specific proteins interact a
 nd which do not? (iii) On evolutionary time scales\, which protein-protein
  interactions are actually conserved across thousands of species? Statisti
 cal inference methods like the Direct-Coupling Analysis (DCA)\, have recen
 tly triggered considerable progress in using sequence data to connect thes
 e different scales\, thereby helping to assemble quaternary protein struct
 ures and to predict conserved interactions between proteins. Besides evide
 nt bioinformatic applications in structural and systems biology\, these me
 thods help to deepen our understanding of the patterns of co-evolution bet
 ween interacting proteins in general.
LOCATION:BSP 727 https://plan.epfl.ch/?room==BSP%20727
STATUS:CONFIRMED
END:VEVENT
END:VCALENDAR