Professor Pletneva received her undergraduate education and M.S. degree in Chemistry from the Higher Chemical College of the Russian Academy of Sciences. She obtained her Ph.D. in Inorganic Chemistry in 2001 from Iowa State University. She then continued her studies at Iowa State University as a postdoc in the group of Professor Amy H. Andreotti exploring structure and dynamics of signaling proteins with NMR spectroscopy. In 2002 Dr. Pletneva joined the research group of Professor Harry B. Gray at the California Institute of Technology, where she has been investigating protein folding dynamics. She will join the faculty of Dartmouth College in the summer of 2007.

Selected Publications

Ekaterina.Pletneva@dartmouth.edu

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Research Interests

In performing their functions, many proteins undergo structural changes that range from subtle conformational fluctuations to massive rearrangements of the polypeptide fold. Our research examines mechanisms of conformational activation in a number of signaling proteins. Protein dynamics are essential to function of the individual signaling proteins and the overall process of signal transduction. We are interested in uncovering the sequence of structural transformations that accompanies changes in the signaling state and understanding the role of protein dynamics in initiation and propagation of the signal.

We employ a variety of experimental techniques, including time-resolved optical and NMR spectroscopy, to observe and quantitatively describe conformational changes, probe protein flexibility, and characterize heterogeneity of protein ensembles. Great emphasis is placed on the application of photochemical and photophysical methods both for triggering and detection of structural changes. Among them, measurements of fluorescence energy transfer kinetics (see publications 1-3 below) and photoinduced electron transfer (see publication 4 below) serve as powerful probes of protein dynamics.

• E. V. Pletneva, H. B. Gray, and J. R. Winkler, "Many faces of the unfolded state. Conformational heterogeneity of unfolded cytochrome c revealed by fluorescence energy transfer kinetics," J. Mol. Biol. 2005, 345, 855-867.
• E. V. Pletneva, H. B. Gray, and J. R. Winkler, "Nature of the cytochrome c molten globule," J. Am. Chem. Soc. 2005, 127, 15370-15371.
• E. V. Pletneva, H. B. Gray, and J. R. Winkler, "Snapshots of cytochrome c folding," Proc. Natl. Acad. Sci. USA 2005, 102, 18397-18402.
• J. C. Lee, J. E. Kim, E. V. Pletneva, J. Faraone-Mennella, H. B. Gray, and J. R. Winkler, "Protein folding, misfolding, and disease," Metal Ions in Life Sciences 2006, 1, 9-60.
• E. V. Pletneva, M. Sundd, D. B. Fulton, and A. H. Andreotti, "Molecular details of Itk activation by prolyl isomerization and phospholigand binding: the NMR structure of the Itk SH2 domain bound to a phosphopeptide," J. Mol. Biol. 2006, 357, 550-561.