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VERSION:2.0
CALSCALE:GREGORIAN
PRODID:UW-Madison-Physics-Events
BEGIN:VEVENT
SEQUENCE:0
UID:UW-Physics-Event-1550
DTSTART:20091009T210000Z
DURATION:PT1H0M0S
DTSTAMP:20260314T200355Z
LAST-MODIFIED:20091001T133543Z
LOCATION:2241 Chamberlin Hall (coffee and cookies at 3:30 pm)
SUMMARY:Protein Intrinsic Disorder and Developmental Biology\, Physics
  Department Colloquium\, Keith Dunker\, Department of Biochemistry and
  Molecular Biology\, Indiana University School of Medicine
DESCRIPTION:The standard view is that each protein's amino acid sequen
 ce provides the information for it to fold into a specific 3D structur
 e\, and this structure is required for its function. Thus\, current bi
 ology and biochemical textbooks suggest that all proteins act via the 
 sequence-to-structure-to-function paradigm. These views are correct fo
 r enzymes\, which function as catalysts that accelerate chemical react
 ions. But a cell is not just a bag of chemical reactions. Biological p
 rocesses\, such as cell division or development of different cell type
 s from a single cell\, require regulation and organization of the vari
 ous chemical reactions. These regulatory functions involve proteins th
 at interact with each other via complex networks.  We used computation
 al and bioinformatics methods to show that the regulatory signaling in
 teractions in cells depend not on protein 3D-structure\, but rather de
 pend on lack of 3D-structure.  For signaling proteins\, we propose a n
 ew paradigm\, given in short as sequence-to-flexible-ensemble-to-funct
 ion.  We will illustrate these ideas using the Wnt signaling pathway\,
  a widespread\, well studied and exemplary signaling network that is c
 rucial for developmental biology.
URL:https://www.physics.wisc.edu/events/?id=1550
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