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SUMMARY:How does Evolution affect Protein Structure Prediction? - Emmy Qin
DTSTART:20151120T122000Z
DTEND:20151120T124000Z
UID:TALK61407@talks.cam.ac.uk
CONTACT:Alex Thom
DESCRIPTION:Can we accurately predict a protein's native structure from am
 ino-acid sequence data alone? A major breakthrough has been the discovery 
 of the imprint of evolutionary constraints in correlated mutations of prot
 ein sequences which can be used to predict residues in contact in 3D space
 . However\, many approaches regard protein family sequences as independent
  samples from a distribution. This is not true - protein sequences share a
 n evolutionary history (phylogeny)\, which 'pollutes' the correlation sign
 al. Here\, we develop a theory of the eigenvalue distribution as a functio
 n of phylogeny\, and furthermore by using Random Matrix Theory we discover
  how to predict this shape.  This allows us to determine precise threshold
 s on the parameters governing evolution and establish parameter regimes wh
 ere evolutionary effects are important.
LOCATION:Unilever Lecture Theatre\, Department of Chemistry
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