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SUMMARY:Unveiling the structure of pathogenic macromolecular machines usin
 g integrative dynamic modeling 
DTSTART:20131211T121500
DTEND:20131211T131000
DTSTAMP:20260510T143316Z
UID:c19b90b2ad1e99e0b3aacc73dd495c0a066dad0c7b8472bbba820d05
CATEGORIES:Conferences - Seminars
DESCRIPTION:Prof. Matteo Dal Peraro\nBio: Matteo Dal Peraro graduated in P
 hysics at the University of Padua in 2000. He obtained his Ph.D. in Biophy
 sics at the International School for Advanced Studies (SISSA\, Trieste) in
  2004. He then received postdoctoral training at the University of Pennsyl
 vania (Philadelphia) under the guidance of Prof. M. L. Klein. He was nomin
 ated Tenure Track Assistant Professor at the EPFL School of Life Sciences 
 in late 2007.\nHis research at the Laboratory for Biomolecular Modeling (L
 BM)\, within the Interfaculty Institute of Bioengineering (IBI)\, focuses 
 on the multiscale modeling of large macromolecular systems.\nProteins ofte
 n assemble in large macromolecular complexes to achieve a specific biologi
 cal task. Unfortunately\, owing to their size and complexity\, these struc
 tures are difficult to determine at atomistic resolution\, preventing thus
  a complete understanding of their mechanism of action.\nIn this talk I wi
 ll present the effort of my laboratory to develop novel ways to predict th
 e structure and function of large biological assemblies. To this end\, we 
 established a new approach that uses swarm intelligence optimization guide
 d by experimental-based restraints to characterize quaternary protein stru
 cture accounting for native dynamics.\nUsing this integrative strategy we 
 were able to reveal the assembly mechanism of aerolysin\, a bacterial pore
 -forming toxin that produces heptameric pores at the target membrane by a 
 concerted swirling motion of its components. In a second study\, we determ
 ined the basal body structure of Yersinia type III secretion system\, disc
 overing how its flexibility is critical for adapting to thickness variatio
 ns at the periplasmic space.\nThe native dynamics of individual components
  emerges\, in these studies\, as the key determinant to define the archite
 cture and understand the function of large multi-protein complexes. Theref
 ore\, the ability of our approach to integrate protein dynamics with spars
 e experimental data is a promising step toward the molecular characterizat
 ion of large pathogenic systems and the design of specific therapeutic str
 ategies.
LOCATION:SV 1717A http://plan.epfl.ch/?lang=en&room=sv+1717+a
STATUS:CONFIRMED
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