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SUMMARY:Using evolutionary sequence variation to make inferences about pro
 tein structure and function - Lucy Colwell\, Chemistry Laboratory\, Univer
 sity of Cambridge
DTSTART:20131018T130000Z
DTEND:20131018T140000Z
UID:TALK47953@talks.cam.ac.uk
CONTACT:Alessio Zaccone
DESCRIPTION:The explosive growth in the number of protein sequences\ngives
  rise to the possibility of using the natural variation in\nsequences of h
 omologous proteins to find residues that control\ndifferent protein phenot
 ypes. Because in many cases phenotypic changes\nare controlled by a group 
 of residues\, the mutations that separate one\nphenotype from another will
  be correlated. We show that correlations\nbetween amino acid mutations at
  different sites in a protein can be\nused to predict\, de novo\, tertiary
  protein structure of both globular\nand transmembrane proteins from large
  sequence alignments.\n\nIn addition\, we find that residues that determin
 e the specificity of\nprotein interactions can be identified. Those amino 
 acids whose\nmutation patterns are most highly constrained in the sequence
  record\nare found to often involve known functional sites of proteins\,\n
 suggesting that correlation analysis may predict functional\nsites from al
 ignments of sequence homologs. Our analysis produces\na probability model 
 for the sequence of a protein\, raising the possibility\nthat we may be ab
 le to identify amino acids that control different protein\nphenotypes\, an
 d hence re-programme existing proteins.
LOCATION:Small Lecture Theatre\, Cavendish Laboratory
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