Professor Juli Feigon received her B.A. from Occidental College and her M.S. and Ph.D. from the University of California, San Diego where she studied with Dr. David Kearns. Her postdoctoral work was completed at the Massachusetts Institute of Technology, where she was a Damon Runyon-Walter Winchell Cancer Fund Postdoctoral Fellow with
Dr. Alexander Rich.
Dr. Feigon has been a UCLA faculty member since 1985, when she was appointed the first female Assistant Professor in the Department of Chemistry and Biochemistry. She currently holds the rank of Distinguished Professor of Biochemistry and the Christopher Foote Term Chair. Her awards and honors include the Dupont Young Faculty Award (1985-1986), Presidential Young Investigator Award of the National Science Foundation (1989-1994), Camille and Henry Dreyfus Teacher/Scholar Award (1990), Glenn T. Seaborg Research Award (1992), Herbert Newby McCoy Award, (1993, 2009, 2022), elected Fellow of the American Association for the Advancement of Science (AAAS) (2002), Elected Member, National Academy of Sciences (2009), Dorothy Crowfoot Hodgkin award of the Protein Society (2017), Biophysical Society Founders Award (2018), and UCLA Academic Senate Diversity, Equity, and Inclusion Research Award (2020), and Finalist, Excellence in Postdoctoral Mentoring Award (2022).
Professor Feigon’s research interests are in structural biology of nucleic acids and their complexes. She pioneered the application of macromolecular NMR spectroscopy to the study of DNA and RNA structure, folding, and interactions with cations, drugs, and proteins. Her laboratory published the first high resolution structures of DNA triplexes, quadruplexes, and aptamers, and her work has provided fundamental insights into DNA A-tract and protein induced bending, cation interactions with DNA, Hoogsteen base pairs, and drug binding to DNA. She has made major contributions to understanding RNA folding and function, including studies of RNA aptamers, ribozymes, and riboswitches, and recognition of RNA by proteins. Her laboratory solved the first NMR structure of a riboswitch and set the standard for high-resolution RNA structures determined by NMR.
For all of this work, she developed new NMR methods and applications for studying nucleic acids structure and dynamics, including assignments and detecting cation interactions. Her work has combined structural and functional studies of RNA–protein complexes to reveal essential determinants of protein recognition of single stranded and of double stranded RNA by RRMs and dsRBDs, respectively. Currently, the Feigon laboratory employs an integrative structural biology approach combining NMR spectroscopy, X-ray crystallography, and electron microscopy (EM) along with biochemistry to study structure, dynamics, assembly, and function of non-coding RNA and RNA-protein complexes, in particular 7SK RNP and telomerase. Over the past two decades, her laboratory pioneered structural studies of telomerase, from solution NMR and X-ray crystal structure and dynamics studies of telomerase RNA and RNA-protein domains of human and Tetrahymena telomerase to the first structure of a telomerase holoenzyme, by negative stain EM at 25 Å resolution, and cryo-EM studies telomerase and associated proteins at increasingly higher resolution.