Ekaterina V. Pletneva

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.

Position: Assistant Professor of Chemistry
E-Mail: Ekaterina V. Pletneva 

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.

Selected Publications

• C. F. Quinn, J. M. Goldberg, and E. V. Pletneva “Protein folding and structural features of protein denatured states. A culminating laboratory experience for biophysical chemistry majors” J. Chem. Ed., in preparation.
• T. G. Moga and E. V. Pletneva “Mapping heme transfer from the Serratia marcescens Soluble Hemophore HasA to its Outer-membrane Receptor HasR” Chemtracts – Inorganic Chemistry, in preparation.
• K. G. Urie, E. V. Pletneva, H. B. Gray, J. R. Winkler, and J. J. Kozak “Electrostatic effects on funneled landscapes and structural diversity in denatured protein ensembles” J. Pept. Sci. 2009, submitted.
• P. Weinkam, E. V. Pletneva, H. B. Gray, J. R. Winkler, and P. G. Wolynes “Electrostatic effects on funneled landscapes and structural diversity in denatured protein ensembles” Proc. Natl. Acad. Sci. U. S. A. 2009, 106, 1796-1801.
• J. L. Taylor, T. G. Moga, O. Karagiaridi, D. E. Wilcox, and E. V. Pletneva “Effects of DNA binding on the structural and redox properties of the [2Fe-2S] transcription factor SoxR” Chemtracts – Inorganic Chemistry, 2008, 21, 336-345.
• E. V. Pletneva, Z. Zhao, T. Kimura, K. V. Petrova, H. B. Gray, and J. R. Winkler “Probing the cytochrome c´ folding landscape” J. Inorg. Biochem. 2007, 101, 1768-1775.
• 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.
• 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, H. B. Gray, and J. R. Winkler “Snapshots of cytochrome c folding” Proc. Natl. Acad. Sci. U. S. A. 2005, 102, 18397-18402.
• E. V. Pletneva, H. B. Gray, and J. R. Winkler “Nature of cytochrome c molten globule” J. Am. Chem. Soc. 2005, 127, 15370-15371.
• 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, M. M. Crnogorac, and N. M. Kostić “Mimicking biological electron transport in sol-gel glass: Photoinduced electron transfer from zinc cytochrome c to plastocyanin or cytochrome c mediated by mobile inorganic complexes” J. Am. Chem. Soc. 2002, 124, 14342-14354.
• E. V. Pletneva, A. T. Laederach, D. B. Fulton, and N. M. Kostić “The role of cation-p interactions in biomolecular association. Design of peptides favoring interactions between cationic and aromatic amino acid side chains” J. Am. Chem. Soc. 2001, 123, 6232-6245.