Santa Fe Institute

Seminar

September 09, 2013
12:15 PM
Collins Conference Room

Debora Marks (Harvard Medical School)

Abstract.  Attributes of living systems are constrained in evolution. An alternative to the analysis of conserved attributes ("characters") is analysis of functional interactions ("'couplings") that cause conservation. A quantitative theory of evolutionary couplings may be widely applicable to biological and technical evolution at different scales of phenomena.  In a particularly interesting application, evolutionary couplings in proteins in the form of amino acid pairwise covariation across a protein family can be used to computationally fold proteins, to predict oligomerization, functional sites and paths, and functionally distinct conformational states. For example, protein residue-residue couplings, used as input to distance geometry and molecular dynamics tools, are sufficient to generate good all-atom models of proteins from different fold classes, including large membrane proteins on a  standard laptop. Since March 2013, a web service at www.EVfold.org provides a tool for the analysis of covaration in proteins with respect to functional interactions and structural distance constraints.

The evolutionary couplings in proteins, extracted from the rich evolutionary sequence record, provide insight into essential interactions constraining protein evolution and broader questions of plasticity and specificity.  I will discuss new work addressing specificity and function as deduced from the evolutionary information. I will also discuss some new theoretical work on the underlying global statistical model used to address biological data types and hope to discuss this with the audience.

Purpose: Research Collaboration

SFI Host: Jennifer Dunne

More Info

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