Dr. Elisa Fadda

Dr. Elisa Fadda
Department of Chemistry and Hamilton Institute
Maynooth University, Ireland

Title: Role of short 3D motifs as the functional keys of intrinsic disorder in protein‐protein interaction

Conformational disorder is now recognized as a distinctive and functional trait of many proteins encoded in the human genome. As a corollary of the “one structure one function” imperative of structural biology, the ability of a protein, or of a protein region, to morph into different shapes, can allow it to play multiple roles by interacting with different partners, thus to expand its functional scope. Conformational plasticity also confers proteins the ability to act as scaffolding units, supporting the reversible formation of multi‐protein assemblies. In my lab we use a variety of molecular simulation techniques to investigate the structural and thermodynamic principles regulating molecular recognition and binding promiscuity in disordered proteins. In this talk I will present and discuss our recent[1‐3] and ongoing work on the characterization of the propensity of intrinsically disordered (ID) regions to form relatively stable, short 3D motifs, which, in addition to random coils, contribute to the experimentally observed structural disorder. I will also discuss how the identification and structural characterization of these 3D motifs by computer simulation can be used as a basis for the rational design of synthetic macrocyclic peptides, as a strategy to develop new diagnostics and therapeutics targeting protein‐protein interactions that involve ID proteins.



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