Special Biochemistry Seminar - Paola Laurino (OIST)

Minimal mutations can dramatically reshape protein function, driving evolution in unexpected ways. In this talk, we explore three natural examples where a few mutations—in the core, on the surface, or within a linker between subdomains—enable proteins to acquire or switch functions. Using biochemical, biophysical, and evolutionary analyses, we uncover the mechanisms behind these shifts. We examine how insertions and deletions (InDels) in Rossmann Fold enzymes switch cofactor specificity, how a short, remote loop insertion in chitinase enables dual functionality, and how a single linker mutation increases affinity by 200-fold in soluble binding proteins. These findings reveal how structural and environmental constraints shape protein evolution, offering insights into protein adaptability and diversification. These findings not only deepen our understanding of protein evolution but also provide strategic insights for protein engineering and functional design.

This event is for Caltech community members only.