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.
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.