Professor of Biochemistry
Focused on a career as a ballet dancer, Rachel took NO classes in science in high school (they interfered with ballet classes and rehearsals!). She danced with the Royal Winnipeg and the Portland Ballet companies for two years after graduating high school and then entered Reed College (Portland Oregon) where she took her first classes in Chemistry, Biology, and Physics and was enthralled. Graduating with a degree in Chemistry, Rachel became the first female Rhodes Scholar from the Pacific Northwest region (using dance as her “sport”), the awards having been opened to women only the year before. This took her to Oxford University where she began a lifelong fascination with NMR and its power to provide unprecedented insights into how proteins work. After a two-year post-doctoral fellowship at Duke University, she moved to University of Washington where she was on the Research Faculty in the Department of Chemistry. There, she used the brand-new techniques of two-dimensional NMR to solve the first de novo protein structure. She was hooked for life. She became Assistant Professor of Biochemistry at University of Washington and has happily remained in the department ever since. She is currently honored to be the Edmond H. Fischer/WRF Chair in Biochemistry.
Research Associate Professor of Biochemistry
Peter is a Research Associate Professor in the Department of Biochemistry. He has a long-standing interest in using biophysical techniques to study protein complexes. He earned his Ph.D. at the University of California, Riverside where he worked on two projects. The first used using rapid-scanning stopped-flow spectroscopy to study the allosteric control of substrate channeling in the Tryptophan Synthase bienzyme complex from Salmonella typhimurium. The second utilized NMR spectroscopy to investigate the conformation of Insulin hexamers in response to the binding of ligands and metals. His growing interest in NMR led him to seek a post-doc position with Rachel Klevit’s group. Working with Rachel, they solved solution of structure of the BRCA1/BARD1 RING domain heterodimer which was subsequently shown to function as a Ubiquitin Ligase. This opened doors to several avenues of research including ongoing studies of BRCA1 and BARD1, the structure and function of Ubiquitin-Conjugating enzymes, and bacterial effector proteins that target or exploit eukaryotic Ubiquitin signaling pathways.
Klevit trainees: Pre-doctoral & Post-doctoral