Daniel Herschlag
Daniel Herschlag
Professor of Biochemistry and, by courtesy, of Chemical Engineering and of Chemistry
RNA and protein enzymes; RNA folding; cellular behavior of RNA/protein complexes
About
The overarching goal of the Herschlag Lab is to understand the fundamental behavior of RNA and proteins and, in turn, how these behaviors determine and impact biology more broadly. We are particularly interested in questions of how enzymes work, how RNA folds, how proteins recognize RNA, and the roles of RNA/protein interactions in regulation and control, and the evolution of molecules and molecular interactions. The lab takes an interdisciplinary approach, spanning and integrating physics, chemistry and biology, and employing a wide range of techniques.
Appointments
Professor, Biochemistry
Professor (By courtesy), Chemistry
Professor (By courtesy), Chemical Engineering
Member, Bio-X
Member, Stanford Cancer Institute
Faculty Fellow, Stanford ChEM-H
Other Appointments
Senior Associate Dean of Graduate Education and Postdoctoral Affairs, School of Medicine (2011 - 2015)
Honors & Awards
Scholar, James B. Angell (Michigan; 1978, 1979)
Phi Beta Kappa, Michigan (1979)
Award in Biochemistry, American Institute of Chemists (SUNY; 1982)
Award for Excellence in Biochemistry, SUNY (1982)
Fellowship, Gillette Foundation (Brandeis; 1986-1987)
Postdoctoral Fellowship, Helen Hay Whitney (Colorado; 1989-1990)
Scholar in Biomedical Science, Lucille P. Markey (1990-1997)
Scholar, Searle (1993-1996)
Fellowship in Science and Engineering, David and Lucile Packard (1995-2000)
Pfizer Award for Enzyme Chemistry, ACS (1997)
Featured Publications
Sigala, P. A., Ruben, E. A., Liu, C. W., Piccoli, P. M. B., Hohenstein, E. G., Martinez, T. J., … Herschlag, D. (2015). Determination of Hydrogen Bond Structure in Water versus Aprotic Environments To Test the Relationship Between Length and Stability. JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 137(17), 5730–5740.
Sunden, F., Peck, A., Salzman, J., Ressl, S., & Herschlag, D. (2015). Extensive site-directed mutagenesis reveals interconnected functional units in the alkaline phosphatase active site. ELIFE, 4.
Sigala, P. A., Fafarman, A. T., Schwans, J. P., Fried, S. D., Fenn, T. D., Caaveiro, J. M. M., … Herschlag, D. (2013). Quantitative dissection of hydrogen bond-mediated proton transfer in the ketosteroid isomerase active site. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 110(28), E2552–E2561.
Natarajan, A., Schwans, J. P., & Herschlag, D. (2014). Using unnatural amino acids to probe the energetics of oxyanion hole hydrogen bonds in the ketosteroid isomerase active site. Journal of the American Chemical Society, 136(21), 7643–7654.
