Using evolutionary sequence variation to make inferences about protein structure and function

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• Lucy Colwell, Chemistry Laboratory, University of Cambridge
• Friday 18 October 2013, 14:00-15:00
• Small Lecture Theatre, Cavendish Laboratory.

If you have a question about this talk, please contact Alessio Zaccone.

The explosive growth in the number of protein sequences gives rise to the possibility of using the natural variation in sequences of homologous proteins to find residues that control different protein phenotypes. Because in many cases phenotypic changes are controlled by a group of residues, the mutations that separate one phenotype from another will be correlated. We show that correlations between amino acid mutations at different sites in a protein can be used to predict, de novo, tertiary protein structure of both globular and transmembrane proteins from large sequence alignments.

In addition, we find that residues that determine the specificity of protein interactions can be identified. Those amino acids whose mutation patterns are most highly constrained in the sequence record are found to often involve known functional sites of proteins, suggesting that correlation analysis may predict functional sites from alignments of sequence homologs. Our analysis produces a probability model for the sequence of a protein, raising the possibility that we may be able to identify amino acids that control different protein phenotypes, and hence re-programme existing proteins.

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