This year’s Nobel Prize in Chemistry was shared by David Baker, a biochemist who received his Ph.D. from UC Berkeley in 1989 working with Randy Schekman, a professor of molecular and cell biology who won the 2013 Nobel Prize in Physiology or Medicine.
At Berkeley, Baker conducted research primarily on protein transport and protein trafficking in yeast, the field in which Schekman received the prize. But after a postdoctoral fellowship at UCSF, he joined the biochemistry faculty at the University of Washington School of Medicine in Seattle and began working on computational methods for predicting and designing the structures and functions of proteins.
In 2003, he used a computer program he had developed named Rosetta to design a totally new protein that was unlike any other known. Baker and colleagues went on to show that a wide range of protein structures could be designed using the Rosetta software.
“Since then, his research group has produced one imaginative protein creation after another, including proteins that can be used as pharmaceuticals, vaccines, nanomaterials and tiny sensors,” according to a press release by the Nobel Foundation. Baker, the foundation noted, “has learned how to master life’s building blocks and create entirely new proteins.”
Baker, 62, received half the prize, while the other half was shared by two scientists — Demis Hassabis and John Jumper — at Google DeepMind in London, who developed a machine learning tool, AlphaFold, that can predict the 3Dl structure of any protein from its amino acid sequence.
A protein’s 3D structure is key to its function, but scientists had struggled since the 1970s to understand how a protein’s amino acid sequence encoded that structure. Then, in 2020, Hassabis and Jumper developed a new version of the AI tool, AlphaFold2.
“With its help, they have been able to predict the structure of virtually all the 200 million proteins that researchers have identified,” according to the Nobel Foundation.
“It’s a truly exciting day for those of us interested in protein folding,” said Susan Marqusee, a Distinguished Professor of molecular and cell biology and of chemistry at UC Berkeley. “David has done as much as any living scientist to chart the path between the amino acid sequences of proteins and their three-dimensional structures. With the ability to design structures at will, the challenge for the future is to incorporate the dynamic movements and structural changes that are required for all sorts of biological function.”