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SUMMARY:Do Complex Neurodegenerative Diseases Follow Simple Chemical Rules
 ? - Prajwal Ciryam\, St John's College
DTSTART:20130513T160000Z
DTEND:20130513T170000Z
UID:TALK45288@talks.cam.ac.uk
CONTACT:Bert Vaux
DESCRIPTION:Neurodegenerative diseases like Alzheimer's\, Parkinson's\, an
 d Huntington's have proved particularly challenging to study because they 
 involve the disruption of a wide variety of cellular processes for reasons
  that are often not obvious. While it is thought that the initiating event
  of these diseases and many others is the folding of specific proteins int
 o an incorrect and toxic shape\, it remains an open question how this lead
 s to a general collapse of protein homeostasis. Over the last 15 years\, h
 owever\, it has become apparent that the principles that govern the misfol
 ding of proteins are general\, leading to the intriguing possibility that 
 even seemingly random disease processes follow from simple chemical princi
 ples. Our current efforts are to bring this knowledge to scale\, seeking t
 o identify bottom-up rules and top-down heuristics to help make sense of d
 isease complexity. Our systems biology effort has recently revealed that s
 upersaturated proteins — those whose concentrations are likely too high 
 to remain soluble in the cell — are particularly at risk for misfolding\
 , and that these proteins are overrepresented in the disparate disease pat
 hways of Alzheimer's\, Parkinson's\, and Huntington's diseases. As Alan Tu
 ring postulated 60 years ago\, biological complexity — both in function 
 and dysfunction — can emerge from relative simplicity. Applying physicoc
 hemical intuition to the large-scale analysis of biological data has the p
 otential to yield important insights about complex disease\, and to help u
 s track the progression of neurodegenerative diseases across whole proteom
 es in patients over their lifetimes.
LOCATION:Keynes Hall\, King's College
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