Nobel Prize in Chemistry 2024 and its Importance for the LIV

The 2024 Nobel Prize in Chemistry was awarded to David Baker for computational protein design, and to Demis Hassabis and John Jumper for their revolutionary algorithms in protein structure prediction. These tools, including RoseTTAFold and AlphaFold2, are also integral to the work of our scientists. At LIV, researchers like Prof. Maya Topf (Head of Research Department Integrative Virology), Prof. Jens Bosse (Associated Group Quantitative and Molecular Virology), and their teams use these methods to better understand protein complexes, such as in their studies on herpesviruses. These developments in structural biology are paving the way for novel therapeutic strategies and drug discovery.

"With AlphaFold's advancements, we can now make highly accurate predictions even for proteins with little homology to known structures," says Maya Topf. "This has greatly advanced our research on viruses like the herpes simplex virus." Jens Bosse adds, "Through our HerpesFolds database, we have made proteome-wide structural predictions for all human herpesviruses, giving us new insights into viral infection mechanisms."

What breakthroughs in the prediction of protein structures can we expect next?

Maya Topf anticipates breakthroughs in the prediction of membrane proteins, which remain difficult to model but are often key drug targets. "Additionally, improving predictions of transient and weak protein interactions, including those with small molecules and nucleic acids, will be crucial for a better understanding of protein function."

Jens Bosse notes that while there will only be incremental improvements in general protein and protein-complex predictions, challenges remain. "Antibody binding is still a challenge, as are interactions with small molecules, DNA, RNA, and post-translational modifications. Moreover, in-silico protein and binder design is still in its infancy, but better algorithms will likely increase experimental success rates. Finally, the interaction of disordered protein domains is still at the beginning stages."