ChemBio seminar by Prof. Paola Laurino - Okinawa Institute of Science and Technology - CH 637
Event details
| Date | 20.06.2025 |
| Hour | 16:15 › 17:15 |
| Speaker | Prof. Paula Laurino |
| Location | |
| Category | Conferences - Seminars |
| Event Language | English |
Title:
How do proteins expand functionality?
Abstract:
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.
Biography:
Prof. Laurino earned her Ph.D. in Organic Chemistry from ETH Zurich (2011), followed by prestigious EMBO and FEBS postdoctoral fellowships at the Weizmann Institute of Science under the mentorship of Professor Dan Tawfik, a pioneer in protein evolution. During her postdoctoral research, she developed fundamental insights into the emergence of protein folds and metabolic pathways.
Since joining OIST as Assistant Professor in 2017 and being promoted to Associate Professor in 2022, Prof. Laurino has established an internationally recognized research program at the interface of protein evolution and engineering. In 2023, she was appointed Visiting Professor at Osaka University's Institute for Protein Research. In 2025, she was awarded the Frontiers Planet Prize as Japan's National Champion for her work on marine bacterial transporters in SAR11.
Website:
https://www.oist.jp/research/research-units/protein
How do proteins expand functionality?
Abstract:
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.
Biography:
Prof. Laurino earned her Ph.D. in Organic Chemistry from ETH Zurich (2011), followed by prestigious EMBO and FEBS postdoctoral fellowships at the Weizmann Institute of Science under the mentorship of Professor Dan Tawfik, a pioneer in protein evolution. During her postdoctoral research, she developed fundamental insights into the emergence of protein folds and metabolic pathways.
Since joining OIST as Assistant Professor in 2017 and being promoted to Associate Professor in 2022, Prof. Laurino has established an internationally recognized research program at the interface of protein evolution and engineering. In 2023, she was appointed Visiting Professor at Osaka University's Institute for Protein Research. In 2025, she was awarded the Frontiers Planet Prize as Japan's National Champion for her work on marine bacterial transporters in SAR11.
Website:
https://www.oist.jp/research/research-units/protein
Practical information
- Informed public
- Free