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SUMMARY:Using evolutionary sequence variation to make inferences about pro
 tein structure and function - Lucy J. Colwell\,  Department of Chemistry\,
  University of Cambridge
DTSTART:20140122T101500Z
DTEND:20140122T111500Z
UID:TALK50421@talks.cam.ac.uk
CONTACT:23791
DESCRIPTION:Abstract: The explosive growth in the number of protein sequen
 ces gives rise to the possibility of using natural variation in sequences 
 of homologous proteins to find residues that control different protein phe
 notypes. Because in many cases phenotypic changes are controlled by a grou
 p of residues\, the mutations that separate one phenotype from another wil
 l be correlated. We show that correlations between amino acid mutations at
  different sites in a protein can be\nused to predict\, de novo\, tertiary
  protein structure of both globular  and transmembrane proteins from large
  sequence alignments. \n\nIn addition\, residues that determine the specif
 icity of protein interactions can be identified from inter-protein residue
  pairs that co-vary. Those amino acids whose mutation patterns are most hi
 ghly constrained by evolution are found to often involve known functional 
 sites of proteins\, such as enzyme active sites\, and ligand binding sites
 .  These findings raise questions about the relationship between protein s
 tructure and function\, and the evolutionary constraints that this relatio
 nship imposes on different proteins.
LOCATION:Biochemistry Seminar Room\, Sanger Building
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