‘The two achievements awarded by the Nobel Committee have revolutionised the science of proteins. They have significantly facilitated the work of modern biotechnology and pharmaceutics, which use proteins as molecular targets, nanosensors, or nanomachines.’ Read the commentary by prof. dr. hab. Krzysztof Liberek of the Intercollegiate Faculty of Biotechnology UG and MUG.

The 2024 Nobel Prize in Chemistry was split in two equal parts and awarded to David Baker of Washington State University for designing and obtaining non-naturally occurring proteins with presumed properties, and to Demis Hassabis and John Jumper of Google DeepMind for predicting protein structures.

This year's prize was awarded for work in the field of protein science. While proteins are synthesised in cells as a linear sequence of amino acids, they need to adopt the right three-dimensional structure to be active. We know that the three-dimensional structure of proteins is determined by the type and order of the amino acids that make them up. So far, it has not been possible to effectively translate information about the type and order of the amino acids that make up a protein into the shape of the folded protein. Understanding the structure of proteins has required labour-intensive and time-consuming experimental methods such as structural X-ray, electron cryomicroscopy, or nuclear magnetic resonance spectroscopy.

Demis Hassabis and John Jumper created the AlphaFold2 programme, which, using artificial intelligence, predicts the three-dimensional structure of proteins based on their amino acid sequence. AlphaFold2 predicts the structure of proteins with significantly higher probability than previously existing computer programmes. The database of structures predicted by this programme contains approximately 200 million proteins. Importantly, these structures are available to researchers and commercial companies. Knowledge of the three-dimensional structures of proteins is the basis for understanding their functions and is of great importance for modern biotechnology and medicine, including in the design of new drugs.

It should be emphasised that the relevance of AlphaFold2, created by Demis Hassabis and John Jumper, as a versatile tool with broad applications in modern life sciences was recognised by the Nobel Committee just three years after the foundations of the programme were created and published in the journal Nature.

David Baker, winner of the second part of the prize, waited 20 years for this recognition. He was the first, in 2003, to create a protein not found in nature with his designed properties and three-dimensional structure. Baker's experimental approach, which uses computational methods to analyse protein structures and folding pathways, enables proteins to be designed and then obtained by expression in living organisms. Using this approach, Baker's team has obtained a number of proteins with presumed desired properties. Such proteins find applications, for example, as nanosensors to detect changes in the environment, components of vaccines or nanomaterials with desired properties.

The two achievements recognised by the Nobel Committee have revolutionised protein science. They have significantly facilitated the work of modern biotechnology and pharmaceuticals, which use proteins as molecular targets, nanosensors, or nanomachines.