BEGIN:VCALENDAR
VERSION:2.0
PRODID:-//Iowa State University CALS LAS Web Team//sites.iastate.edu//EN
BEGIN:VEVENT
UID:20240426T202000-943-www.chem.iastate.edu
DTSTART:20240426T202000Z
SEQUENCE:0
TRANSP:OPAQUE
DTEND:20240426T212000Z
LOCATION:1352 Gilman
SUMMARY:Paul Robustelli - \"Targeting Intrinsically Disordered Proteins and
  Biomolecular Condensates with Small Molecule Drugs\" (BioPhysical)
CLASS:PUBLIC
DESCRIPTION:Paul RobustelliDartmouth CollegeHosted by: Vincenzo Venditti**B
 ioPhysical Seminar**Targeting Intrinsically Disordered Proteins and Biomol
 ecular Condensates with Small Molecule DrugsAbstract:Intrinsically disorde
 red proteins (IDPs)\, which represent ~40% of the human proteome\, play cr
 ucial roles in a variety of biological pathways and biomolecular assemblie
 s and have been implicated in many human diseases. IDPs do not fold into a
  well-defined three-dimensional structure under physiological conditions. 
 Instead\, they populate a dynamic conformational ensemble of rapidly inter
 converting structures. As a result\, IDPs are extremely difficult to exper
 imentally characterize and are largely considered “undruggable” by con
 ventional structure-based drug design methods.&nbsp\; Our laboratory utili
 zes a combination of computational and biophysical methods to characterize
  the molecular recognition mechanisms of intrinsically disordered proteins
  in atomic detail.&nbsp\; Here I will discuss recent progress in our effor
 ts to characterize the interactions of IDPs with small molecule drugs\, un
 derstand molecular mechanisms that drive the formation of biomolecular con
 densate\, and understand how small molecule drugs modulate biomolecular co
 ndensate stability.&nbsp\;Bio:Paul Robustelli\, PhD.&nbsp\;is an assistant
  professor of chemistry at Dartmouth College\, where his research focuses 
 on the integration of computational and experimental methods to study dyna
 mic and disordered proteins. Dr. Robustelli utilizes computer simulations 
 and nuclear magnetic resonance (NMR) spectroscopy to model the conformatio
 nal ensembles of intrinsically disordered proteins at atomic resolution to
  understand how small molecule drugs bind and inhibit disordered proteins 
 and rationally design novel disordered protein inhibitors. Dr. Robustelli 
 has made contributions to the development of physical models (“force fie
 lds”) that enable accurate simulations of disordered proteins and comput
 ational methods to integrate NMR data as restraints in molecular simulatio
 ns.Dr. Robustelli earned his B.A. in chemistry from Pomona College and his
  Ph.D. in chemistry from the University of Cambridge in the laboratory of 
 Michele Vendruscolo.&nbsp\; Before joining the chemistry faculty at Dartmo
 uth\, Paul worked as a postdoctoral fellow at Columbia University in the l
 aboratory of Arthur Palmer III and as a scientist at D.E. Shaw Research.\n
 \nMore information at: https://www.chem.iastate.edu/event/2024/paul-robust
 elli-targeting-intrinsically-disordered-proteins-and-biomolecular-condensa
 tes
DTSTAMP:20260312T142550Z
END:VEVENT
END:VCALENDAR