A Seattle family of scientists
David Baker was born on October 6, 1962, in Seattle, Washington, into a Jewish family of scientists. His father, Marshall Baker, was a theoretical physicist who joined the University of Washington faculty in 1962, and his mother, Marcia Bourgin Baker, was a geophysicist who became a professor of geophysics and atmospheric sciences there, known for research on cloud physics. He grew up in Seattle and graduated from the city’s Garfield High School.
Science was not his first plan. When he went to Harvard University, he chose philosophy and social studies. Then, during a course in evolutionary biology, he came across the first edition of the textbook Molecular Biology of the Cell, and it changed the direction of his life. He switched to biology and graduated in 1984.
Learning how proteins fold
Baker earned his doctorate in biochemistry at the University of California, Berkeley, in 1989, in the laboratory of Randy Schekman, a future Nobel laureate, studying how proteins are moved around inside yeast cells. He then did postdoctoral work in biophysics with David Agard at the University of California, San Francisco, where he became fascinated by one of the great puzzles of biology: how a protein folds.
Proteins are the working machines of life. Each is a chain of amino acids, drawn from an alphabet of twenty, that folds up into a precise three-dimensional shape, and that shape determines what the protein does: digest food, carry oxygen, fight infection, send signals between cells. Since the 1960s scientists had known that the sequence of amino acids alone determines the shape, but predicting the shape from the sequence had proved fiendishly difficult.
Rosetta
In 1993 Baker returned home to Seattle as a faculty member in the biochemistry department of the University of Washington School of Medicine, where he has worked ever since. He began with experiments on how small proteins fold and used what he learned to write computer software that could predict a protein’s structure. The program was called Rosetta. In 1998 Baker entered it in CASP, the biennial competition in which research groups predict protein structures before they are revealed, and it did remarkably well.
Baker made Rosetta’s code available to researchers, and a global community of laboratories, organised as the Rosetta Commons, extended it for many purposes. He also brought the public into the work. Rosetta@home, launched in the mid-2000s, let volunteers donate spare computer time to protein calculations, and Foldit, a computer game developed with colleagues in computer science, invited players to fold proteins by hand; in 2011 Foldit players helped work out the structure of an enzyme from a virus related to HIV that had puzzled scientists for years.
Rosetta became one of the most widely used tools in structural biology. Scientists used it to model the shapes of proteins whose structures had not been determined experimentally, to design changes that make enzymes or antibodies work better, and to help solve experimental structures. Baker’s group competed in CASP year after year, concentrating on the hardest category, predicting structures from scratch without a known template.
Running the software in reverse
Success at prediction gave Baker a bold idea. If Rosetta could take a sequence and predict a shape, perhaps it could be run backwards: start with a shape that had never existed and ask what sequence of amino acids would fold into it. Most protein engineers at the time modified natural proteins. Baker wanted to design them from first principles, comparing his approach to building aircraft from the laws of aerodynamics rather than by modifying birds.
In 2003 his group reported Top7, a protein of 93 amino acids with a fold that does not occur anywhere in nature. They drew the structure, let Rosetta compute a sequence, produced the protein in bacteria and determined its structure by X-ray crystallography. It matched the design almost exactly. The Nobel committee would later describe this as achieving the almost impossible: building entirely new kinds of proteins.
Proteins made to order
Designed proteins can do things natural ones cannot. Because every atom is planned, they can be made unusually stable, able to survive heat that would destroy natural proteins, which makes them easier to store and ship. They can be shaped to fit a single target, such as a viral protein or a toxin, very tightly, and they can be built to assemble themselves into precise structures such as hollow cages or particles that display many copies of a vaccine target at once. The Nobel committee pointed to pharmaceuticals, vaccines, nanomaterials and tiny sensors as fields where such proteins are already being used.
From Top7 onward, Baker’s laboratory and the Institute for Protein Design, which he founded and directs at the University of Washington, have produced a stream of designed proteins: enzymes for new chemical reactions, tiny sensors, self-assembling cages and nanoparticles, molecules that bind tightly to chosen targets, and new materials. After the artificial-intelligence breakthroughs of 2020 in protein structure prediction, Baker’s group built deep-learning tools of its own, including RoseTTAFold for predicting structures and RFdiffusion for generating new designs, and shared them freely with researchers worldwide.
These methods have been used to design potential medicines and vaccines against viruses including influenza and SARS-CoV-2, and in 2025 his group reported designed proteins that neutralise lethal snake venom toxins in mice, raising hopes of cheaper, more effective antivenoms for the regions where snakebite kills most. Baker has co-founded more than a dozen biotechnology companies to carry designs toward patients, among them Icosavax, which developed vaccines based on designed nanoparticles.
A vaccine built by design
The clearest proof of the field’s promise came during the COVID-19 pandemic. Scientists at the Institute for Protein Design, led by Neil King and David Veesler, used computationally designed proteins that assemble themselves into tiny particles studded with 60 copies of a key fragment of the coronavirus spike protein. The South Korean company SK bioscience developed the vaccine, with support from the Coalition for Epidemic Preparedness Innovations and an adjuvant from GlaxoSmithKline.
In June 2022 South Korea approved it for adults under the name SKYCovione, which the institute describes as the world’s first computationally designed protein medicine. In a trial of 4,037 adults it produced roughly three times more neutralising antibodies than the Oxford/AstraZeneca vaccine. It was later approved in the United Kingdom and granted Emergency Use Listing by the World Health Organization. The University of Washington licensed the technology royalty-free for the duration of the pandemic, and the vaccine was designed to be stable without deep freezing, making it easier to use where cold storage is scarce.
The approach behind SKYCovione, displaying many copies of a viral fragment on a designed protein scaffold, is being applied to other diseases. Icosavax, the company Baker co-founded, used designed nanoparticles to develop vaccine candidates against respiratory viruses including RSV, a leading cause of serious illness in babies and older adults, and was acquired by AstraZeneca in 2023.
The Nobel Prize
On October 9, 2024, the Royal Swedish Academy of Sciences awarded Baker one half of the Nobel Prize in Chemistry “for computational protein design”; the other half went to Demis Hassabis and John Jumper of Google DeepMind for the AlphaFold system that predicts protein structures. The academy said the abilities to predict protein structures and to design new proteins confer the greatest benefit to humankind, and it listed pharmaceuticals, vaccines, nanomaterials and tiny sensors among the products of Baker’s work.
His other honours include the Feynman Prize in Nanotechnology (2004), the Sackler International Prize in Biophysics (2008), the Breakthrough Prize in Life Sciences (2021) and the BBVA Foundation Frontiers of Knowledge Award (2022). He is an investigator of the Howard Hughes Medical Institute and a member of the U.S. National Academy of Sciences, and in 2024 Time magazine named him one of the most influential people in health.
Family, faith and a collaborative style
Baker was born into a Jewish family, and he grew up in a household where both parents were working scientists. He has not made religious practice a public part of his story. He is married to Hannele Ruohola-Baker, a biochemist and stem-cell researcher who is also a professor at the University of Washington; they have two children.
He is known for running an unusually large and open laboratory and for sharing tools rather than guarding them. Many of his former students and postdoctoral fellows now lead their own groups around the world, and the software he released has been taken up by thousands of researchers. In a 2019 TED talk he described five challenges, from vaccines to new materials, that designed proteins might help solve.
Legacy
For most of history, humanity could only use the proteins that evolution had made. David Baker showed that we can write new ones. His work has turned protein design from a dream into a working engineering discipline, and its first fruits, a COVID-19 vaccine made of designed particles, candidate antivenoms and a growing list of experimental medicines, are already reaching the clinic.
The Nobel committee summed it up simply: life could not exist without proteins, and we can now design our own. The consequences, for vaccines that can be designed in weeks, medicines aimed precisely at disease, and greener chemistry, are only beginning to unfold.
Sources & further reading
Press release: The Nobel Prize in Chemistry 2024, NobelPrize.org · Popular information: The Nobel Prize in Chemistry 2024, NobelPrize.org · COVID-19 vaccine with IPD nanoparticles wins full approval abroad, UW Institute for Protein Design · David Baker (biochemist), Wikipedia · Researched from the sources above and checked against them. Spotted an error? Tell us.
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