Professor Todd Yeates earned his PhD at UCLA developing X-ray crystallographic methods while working on early structures of membrane proteins, followed by postdoctoral research at the Scripps Research Institute elucidating the structures of viral capsids. Yeates joined the faculty at UCLA, where his research combines interests in molecular biology, biophysics and computational methods, applied to problems from molecular structure to genomic sequence analysis.
Current research in the lab focuses on large protein assemblies, including those found in nature and those that can be created in the laboratory by design. Research in the Yeates group laid out a structural understanding of protein-based metabolic organelles in bacteria, often called ‘bacterial microcompartments’. On the design side, the Yeates group developed the first methods for designing highly symmetric self-assembling protein materials, such cubic cages, which are now finding applications in biomedicine, imaging, and biomaterials design.
Advances in computational genomics made by the group include the development of algorithms for inferring cellular functions for vast numbers of protein sequences using ‘non‐homology’ methods, which introduced a new paradigm for mining genomic data. Advances in theory and methods for structural biology include the development of universally used equations for analyzing diffraction data, a solution to the decades-old problem of why proteins crystallize in strongly favored symmetries, and development of protein-based scaffolds for cryo-EM imaging of small proteins. Yeates is the Director of the UCLA DOE-Institute for Genomics and Proteomics.
Molecular, Structural and Computational biology
Research in the Yeates laboratory covers the areas of molecular, structural and computational biology and design.
Much of the group’s current research focuses on a deep understanding of protein structures and large assemblies, with an emphasis on the underlying principles that guide their behavior and evolution, and which enable the atomic level design of novel self-assembling protein architectures.
Our studies of natural self-assembling protein architectures have focused on a remarkable but still not well-appreciated family of giant protein capsids inside many bacterial cells. Our structural studies on the carboxysome and related bacterial microcompartments laid out a mechanistic understanding for these extraordinary structures, showing that bacteria do possess true organelles.
In our frontier bioengineering studies, we are designing entirely novel protein architectures, including cubic cages and extended crystalline arrays in two and three dimensions. Various types of protein assemblies, natural and designed, are finding applications as active enzymatic materials, imaging scaffolds, and biotherapeutics.
Honors & Awards
- University of California Regents Scholarship
- NSF Presidential Young Investigator
- Sidhu Award – Pittsburgh Diffraction Society
- McCoy Award for Excellence in Research – UCLA Chemistry
- Plenary Lecture – German Crystallographic Society
- Fellow of the American Association for the Advancement of Science
- Hansen-Dow Award for Excellence in Teaching – UCLA Chemistry
- Keynote Address – Foundations of Nanoscience
- Program Chair – Annual Meeting of the Protein Society
- American Society for Biochemistry and Molecular Biology – Delano Award in Computational Biosciences
- Xinda Lecturer – Peking University