Professor David Baker awarded the Nobel Prize in Chemistry 2024
- Post by: CIPPS
- 8 November 2024
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CIPPS Partner Investigator, Professor David Baker, who serves as Professor of Biochemistry at the University of Washington, Seattle WA, USA, was recently named recipient of the Nobel Prize in Chemistry in acknowledgment of his achievement “for computational protein design.”
The 2024 Nobel Prize in Chemistry was awarded one half to David Baker and the other half jointly to Demis Hassabis and John Jumper of Google DeepMind, London, UK. This year’s award is not just about proteins, it emphasizes the progressive breakthroughs in solving the structural prediction problem of proteins by using reliable and robust technologies, such as A.I. models and computational software. This can aid researchers to accurately and efficiently design, develop, and predict new-to-nature protein macromolecules. These in silico methods have been demonstrated to work synergistically with interdisciplinary researchers, tackling the global human health crisis, by providing access to a larger reservoir of therapeutic molecules.
David Baker is a leading international expert in computational chemistry and has made major contributions to the field of protein structural prediction of unknown macromolecules. The Baker research group also develops protein design software to create new molecules aimed to solve pressing global challenges in medicine, technology, and sustainability. By iterating between computation and hands-on laboratory experiments, the Baker group strives to continually improve their protein design methodologies.
Peptides and proteins are the working molecules of life. They make up the basic biological machinery that is responsible for many physiological processes. Peptides and proteins can change the shape and structure of cells and tissues, and regulate life cycle functions such as development, growth, maturation, reproduction, ageing and death. Although these biological macromolecules have a set of diverse functionalities, there remains a challenge in designing new-to-nature bio-active proteins. A revolutionary breakthrough in de novo protein design was reported by David Baker and coworkers in the early 2000s, showcasing a 93-residue α/β protein, called Top7, with a novel sequence and topology. Top7 was generated using their in-house software, called the Rosetta program, which was initially focused on ab initio structure prediction of small proteins. The Rosetta program has now become a household software many biochemists are using for protein structural predictions.
Top7 is a remarkable achievement because it was a project with many firsts. It was the first:
- large protein with two α-helices and a β-sheet where its predicted structure was proven by the experimental data.
- first novel globular protein intentionally designed with a folding pattern not found in the Protein Data Bank, and
- new-to-nature macromolecule designed to have no significant sequence similarity to any naturally occurring protein in the sequence database.
Since its debut, the Rosetta program has been licensed commercially to over 27 biotechnology and pharmaceutical companies, including Johnson & Johnson, Pfizer, Merck, and Monsanto.
The Nobel Prize in Chemistry is announced annually by the Royal Swedish Academy of Sciences to recognise international researchers encompassing all disciplines of chemistry, for work that has “the greatest benefit to humankind.” Each Nobel Prize laureate is awarded with a medal, a personal diploma, and a monetary award set at Swedish kronor (SEK) of 11.0 million per full Nobel Prize.
The team at CIPPS would like to send our heartiest congratulations to Professor David Baker on his incredible life-time achievement.
Resources:
Kuhlman, B.; Dantas, G.; Ireton, G.C.; Varani, G.; Stoddard, B.L.; Baker, D. Design of a novel globular protein fold with atomic-level accuracy. Science 2003, 302, 1364-1368.
- Simons, K.T.; Bonneau, R.; Ruczinski, I.; Baker, D. Ab initio protein structure prediction of CASPIII targets using ROSETTA. Proteins: Struct. Funct. Genet. Suppl. 1999, 3, 171-176.