BEGIN:VCALENDAR
VERSION:2.0
PRODID:-//Talks.cam//talks.cam.ac.uk//
X-WR-CALNAME:Talks.cam
BEGIN:VEVENT
SUMMARY:Using evolutionary sequence variation to make inferences about pro
 tein structure and function - Colwell\, L (University of Cambridge)
DTSTART:20140317T143000Z
DTEND:20140317T151000Z
UID:TALK51455@talks.cam.ac.uk
CONTACT:Mustapha Amrani
DESCRIPTION:The explosive growth in the number of protein sequences gives 
 rise to the possibility of using natural variation in sequences of homolog
 ous proteins to find residues that control different protein phenotypes. B
 ecause in many cases phenotypic changes are controlled by a group of resid
 ues\, the mutations that separate one phenotype from another will be corre
 lated. We show that correlations between amino acid mutations at different
  sites in a protein can be used to predict\, de novo\, tertiary protein st
 ructure of both globular and transmembrane proteins from large sequence al
 ignments.\n \nIn addition\, residues that determine the specificity of pro
 tein interactions can be identified from inter-protein residue pairs that 
 co-vary. Those amino acids whose mutation patterns are most highly constra
 ined by evolution are found to often involve known functional sites of pro
 teins\, such as enzyme active sites\, and ligand binding sites. These find
 ings raise questions about the relationship between protein structure and 
 function\, and the evolutionary constraints that this relationship imposes
  on different proteins.\n \nOur maximum entropy based analysis identifies 
 a global probability with a minimal set of amino acid pair interactions th
 at reproduce all the observed pairwise correlations in the data. The resul
 ting probability model for the sequence of the protein of interest raises 
 the possibility that we may be able to identify amino acids that control d
 ifferent protein phenotypes\, and hence re-programme existing proteins.\n
LOCATION:Seminar Room 1\, Newton Institute
END:VEVENT
END:VCALENDAR