David Baker, a renowned biochemist who earned his Ph.D. from UC Berkeley in 1989, has been honored with the prestigious Nobel Prize in Chemistry this year. Baker completed his doctoral work under the guidance of Professor Randy Schekman, a 2013 Nobel Laureate in Physiology or Medicine, focusing on protein transport and trafficking in yeast. Schekman, reflecting on Baker’s contributions, remarked, “David’s brilliance, energy, and creativity elevated the work in my laboratory, enabling us to tackle protein secretion with a biochemical approach that complemented our genetic analysis.”
Baker’s journey didn’t end there. Following a postdoctoral fellowship at UCSF, he became a faculty member at the University of Washington School of Medicine. His pioneering work on computational methods to predict and design protein structures and functions revolutionized the field. In 2003, Baker achieved a breakthrough by creating a novel protein using a computer program called Rosetta, an innovation unlike any existing protein. This achievement opened doors to the design of an array of unique protein structures, with Rosetta playing a central role.
The Nobel Foundation’s announcement highlighted the diversity of Baker’s groundbreaking work. His group has continued to design imaginative proteins with potential applications in pharmaceuticals, vaccines, nanomaterials, and even microscopic sensors. “Baker has mastered life’s fundamental building blocks, crafting entirely new proteins,” the foundation stated. Schekman further praised Baker’s work, noting how his team at the University of Washington developed Rosetta into a powerful tool that addresses a long-standing challenge: how proteins fold into their specific three-dimensional forms.
At 62, David Baker shares the prize with two other distinguished scientists, Demis Hassabis and John Jumper from Google DeepMind in London, recognized for their development of AlphaFold. This revolutionary machine-learning tool, launched in 2020, predicts the 3D structure of proteins from their amino acid sequences—a problem that has baffled scientists for decades. The team’s AlphaFold2 tool has since mapped the structures of nearly 200 million proteins, transforming our understanding of protein folding.
UC Berkeley’s Professor Susan Marqusee praised Baker’s contributions to the field. “David has charted the path between amino acid sequences and their three-dimensional configurations like no other. The next challenge lies in embracing the dynamic motions and structural shifts essential to biological functions.”
Baker’s indomitable spirit and creative genius have undeniably reshaped the landscape of biochemistry, pushing the boundaries of what is possible in protein design and molecular biology. His work, alongside that of Hassabis and Jumper, has provided the scientific community with invaluable tools, offering fresh insights into the intricate world of protein folding.