Ph.D.: University of California at Berkeley, 1980 Postdoctoral Fellow: NATO Fellow, 1982-83

Molecular Biophysics Nucleic Acids Structural Biology Biophysics

Professor Pardi's primary research interests are in the area of biophysical chemistry and NMR spectroscopy. High-resolution multi-dimensional NMR experiments are used to probe the structure and dynamics of biomolecules in solution. The Pardi group also continues to develop improved methods for determining the solution structures of proteins and RNAs. A long-range goal is to understand the relationship between the structures (and dynamics) of these molecules and their biological functions.

Lee, J. H., Canny, M. D., De Erkenez, A., Krilleke, D., Ng, Y. S., Shima, D. T., Pardi, A. & Jucker, F. (2005). A therapeutic aptamer inhibits angiogenesis by specifically targeting the heparin binding domain of VEGF(165). Proc. Natl. Acad. Sci. U. S. A. 102, 18902-18907. Downey, C. D., Fiore, J. L., Stoddard, C. D., Hodak, J. H., Nesbitt, D. J. & Pardi, A. (2006). Metal Ion Dependence, Thermodynamics, and Kinetics for Intramolecular Docking of a GAAA Tetraloop and Receptor Connected by a Flexible Linker. Biochemistry 45, 3664-73. Latham, M. P. & Pardi, A. (2009). Measurement of imino H-1-H-1 residual dipolar couplings in RNA. J. Biomol. NMR 43, 121-129. Latham, M. P., Zimmermann, G. R. & Pardi, A. (2009). NMR Chemical Exchange as a Probe for Ligand-Binding Kinetics in a Theophylline-Binding RNA Aptamer. J. Am. Chem. Soc. 131, 5052-5053. Warner, L. R., Varga, K., Lange, O. F., Baker, S. L., Baker, D., Sousa, M. C. & Pardi, A. (2011). Structure of the BamC Two-Domain Protein Obtained by Rosetta with a Limited NMR Data Set. J. Mol. Biol. 411, 83-95.