David Baker | |
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Born | Seattle, Washington, U.S. | October 6, 1962
Alma mater | |
Known for | |
Spouse | Hannele Ruohola-Baker |
Awards |
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Scientific career | |
Fields | Computational biology |
Institutions | |
Thesis | Reconstitution of intercompartmental protein transport in yeast extracts (1989) |
Doctoral advisor | Randy Schekman |
Other academic advisors | David Agard |
Doctoral students | Richard Bonneau |
Other notable students | Brian Kuhlman, Tanja Kortemme |
Website | www |
David Baker (born October 6, 1962) is an American biochemist and computational biologist who has pioneered methods to design proteins and predict their three-dimensional structures. He is the Henrietta and Aubrey Davis Endowed Professor in Biochemistry, an investigator with the Howard Hughes Medical Institute, and an adjunct professor of genome sciences, bioengineering, chemical engineering, computer science, and physics at the University of Washington. He was awarded the shared 2024 Nobel Prize in Chemistry for his work on computational protein design. [3] [4]
Baker is a member of the United States National Academy of Sciences and the director of the University of Washington's Institute for Protein Design. [5] He has co-founded more than a dozen biotechnology companies and was included in Time magazine's inaugural list of the 100 Most Influential People in health in 2024. [6]
Baker was born into a Jewish family in Seattle, Washington on October 6, 1962, the son of physicist Marshall Baker and geophysicist Marcia (née Bourgin) Baker. [7] He graduated from Seattle's Garfield High School. [8]
Baker received a Bachelor of Arts degree with a major in biology from Harvard University in 1984. He then joined the laboratory of Randy Schekman, where he worked primarily on protein transport and trafficking in yeast, and obtained a Doctor of Philosophy in biochemistry from the University of California, Berkeley in 1989. [9] In 1993, he completed his postdoctoral training in biophysics with David Agard at the University of California, San Francisco.
Baker joined the Department of Biochemistry at the University of Washington School of Medicine as a faculty member in 1993. He became a Howard Hughes Medical Institute investigator in 2000. [10] Baker was elected a Fellow of the American Academy of Arts and Sciences in 2009. [11]
Baker is married to Hannele Ruohola-Baker, another biochemist at the University of Washington. They have two children.
Although primarily known for the development of computational methods for predicting and designing the structures and functions of proteins, Baker maintains an active experimental biochemistry group. [12] He has authored over 600 scientific papers. [13]
Baker's group developed the Rosetta algorithm for ab initio protein structure prediction, which has been extended into a tool for protein design, a distributed computing project called Rosetta@home, [12] [14] [15] and the computer game Foldit. [16] [17] [18] Baker served as the director of the Rosetta Commons, a consortium of labs and researchers that develop biomolecular structure prediction and design software. Baker's group has regularly competed in the CASP structure prediction competition, specializing in ab initio methods, including both manually assisted and automated variants of the Rosetta protocol. [19] [20] Using artificial intelligence, his group has developed later a newer version of the program known as RoseTTAFold. [21] [22]
Baker's group is also active in the field of protein design; [12] [23] they are noted for designing Top7, the first artificial protein with a novel fold. [24]
In 2017, Baker's Institute for Protein Design received over $11 million from Open Philanthropy, [25] [26] followed by an additional $3 million donation in 2021. [27]
In April 2019, Baker gave a TED talk titled "5 challenges we could solve by designing new proteins" at TED2019 in Vancouver, Canada. [28]
Baker has co-founded several biotechnology companies, including Prospect Genomics which was acquired by an Eli Lilly subsidiary in 2001, [29] Icosavax which was acquired by AstraZeneca in 2023, [30] Sana Biotechnology, Lyell Immunotherapeutics, and Xaira Therapeutics.
For his work on protein folding, Baker has received numerous awards, including the Overton Prize (2002), [31] the Sackler International Prize in Biophysics (2008), [32] the Wiley Prize (2022) [33] and the BBVA Foundation Frontiers of Knowledge Award in the category "Biology and Biomedicine" (2022). [34]
For his work on protein design, Baker has received the Newcomb Cleveland Prize (2004), [35] the Feynman Prize in Nanotechnology (2004), [36] and the Breakthrough Prize in Life Sciences (2021). [37]
In 2024, Baker was awarded half of the Nobel Prize in Chemistry for his work on protein design; the other half went to John M. Jumper and Demis Hassabis for development of AlphaFold, a program for protein structure prediction. [3] [4]
Structural biology, as defined by the Journal of Structural Biology, deals with structural analysis of living material at every level of organization.
Levinthal's paradox is a thought experiment in the field of computational protein structure prediction; protein folding seeks a stable energy configuration. An algorithmic search through all possible conformations to identify the minimum energy configuration would take an immense duration; however in reality protein folding happens very quickly, even in the case of the most complex structures, suggesting that the transitions are somehow guided into a stable state through an uneven energy landscape.
Top7 is an artificial protein, classified as a de novo protein. This means that the protein itself was designed to have a specific structure and functional properties.
The Human Proteome Folding Project (HPF) is a collaborative effort between New York University, the Institute for Systems Biology (ISB) and the University of Washington, using the Rosetta software developed by the Rosetta Commons. The project is managed by the Bonneau lab.
Protein design is the rational design of new protein molecules to design novel activity, behavior, or purpose, and to advance basic understanding of protein function. Proteins can be designed from scratch or by making calculated variants of a known protein structure and its sequence. Rational protein design approaches make protein-sequence predictions that will fold to specific structures. These predicted sequences can then be validated experimentally through methods such as peptide synthesis, site-directed mutagenesis, or artificial gene synthesis.
Rosetta@home is a volunteer computing project researching protein structure prediction on the Berkeley Open Infrastructure for Network Computing (BOINC) platform, run by the Baker lab. Rosetta@home aims to predict protein–protein docking and design new proteins with the help of about fifty-five thousand active volunteered computers processing at over 487,946 GigaFLOPS on average as of September 19, 2020. Foldit, a Rosetta@home videogame, aims to reach these goals with a crowdsourcing approach. Though much of the project is oriented toward basic research to improve the accuracy and robustness of proteomics methods, Rosetta@home also does applied research on malaria, Alzheimer's disease, and other pathologies.
Sir Demis Hassabis is a British artificial intelligence (AI) researcher, and entrepreneur. He is the chief executive officer and co-founder of Google DeepMind, and Isomorphic Labs, and a UK Government AI Adviser. In 2024, Hassabis and John M. Jumper were jointly awarded the Nobel Prize in Chemistry for their AI research contributions for protein structure prediction.
Michael Levitt, is a South African-born biophysicist and a professor of structural biology at Stanford University, a position he has held since 1987. Levitt received the 2013 Nobel Prize in Chemistry, together with Martin Karplus and Arieh Warshel, for "the development of multiscale models for complex chemical systems". In 2018, Levitt was a founding co-editor of the Annual Review of Biomedical Data Science.
In computational biology, de novo protein structure prediction refers to an algorithmic process by which protein tertiary structure is predicted from its amino acid primary sequence. The problem itself has occupied leading scientists for decades while still remaining unsolved. According to Science, the problem remains one of the top 125 outstanding issues in modern science. At present, some of the most successful methods have a reasonable probability of predicting the folds of small, single-domain proteins within 1.5 angstroms over the entire structure.
A dry lab is a laboratory where the nature of the experiments does not involve significant risk. This is in contrast to a wet lab where it is necessary to handle various types of chemicals and biological hazards. An example of a dry lab is one where computational or applied mathematical analyses are done on a computer-generated model to simulate a phenomenon in the physical realm. Examples of such phenomena include a molecule changing quantum states, the event horizon of a black hole or anything that otherwise might be impossible or too dangerous to observe under normal laboratory conditions. This term may also refer to a lab that uses primarily electronic equipment, for example, a robotics lab. A dry lab can also refer to a laboratory space for the storage of dry materials.
Foldit is an online puzzle video game about protein folding. It is part of an experimental research project developed by the University of Washington, Center for Game Science, in collaboration with the UW Department of Biochemistry. The objective of Foldit is to fold the structures of selected proteins as perfectly as possible, using tools provided in the game. The highest scoring solutions are analyzed by researchers, who determine whether or not there is a native structural configuration that can be applied to relevant proteins in the real world. Scientists can then use these solutions to target and eradicate diseases and create biological innovations. A 2010 paper in the science journal Nature credited Foldit's 57,000 players with providing useful results that matched or outperformed algorithmically computed solutions.
Gajendra Pal Singh Raghava is an Indian bio-informatician and head of computational biology at the Indraprastha Institute of Information Technology.
Frances Hamilton Arnold is an American chemical engineer and Nobel Laureate. She is the Linus Pauling Professor of Chemical Engineering, Bioengineering and Biochemistry at the California Institute of Technology (Caltech). In 2018, she was awarded the Nobel Prize in Chemistry for pioneering the use of directed evolution to engineer enzymes.
Richard Bonneau is an American computational biologist and data scientist whose primary research is in the following areas: learning networks from functional genomics data, predicting and designing protein and peptiodomimetic structure and applying data science to social networks. A professor at New York University, he holds appointments in the department of biology, the Center for Data Science and the Courant Institute of Mathematical Sciences.
Ram Samudrala is a professor of computational biology and bioinformatics at the University at Buffalo, United States. He researches protein folding, structure, function, interaction, design, and evolution.
David Tudor Jones is a Professor of Bioinformatics, and Head of Bioinformatics Group in the University College London. He is also the director in Bloomsbury Center for Bioinformatics, which is a joint Research Centre between UCL and Birkbeck, University of London and which also provides bioinformatics training and support services to biomedical researchers. In 2013, he is a member of editorial boards for PLoS ONE, BioData Mining, Advanced Bioinformatics, Chemical Biology & Drug Design, and Protein: Structure, Function and Bioinformatics.
AlphaFold is an artificial intelligence (AI) program developed by DeepMind, a subsidiary of Alphabet, which performs predictions of protein structure. The program is designed as a deep learning system.
Jens Meiler is a German-American biologist and structural chemist. He currently serves as a Professor of Chemistry and Associate Professor of Pharmacology and Biomedical Informatics at Vanderbilt University. His research focuses on protein structures and computational biology, drawing on interdisciplinary techniques from other sciences.
John Michael Jumper is an American chemist and computer scientist. He currently serves as director at Google DeepMind. Jumper and his colleagues created AlphaFold, an artificial intelligence (AI) model to predict protein structures from their amino acid sequence with high accuracy. Jumper stated that the AlphaFold team plans to release 100 million protein structures.