Elizabeth Rhoades PhD

Associate Professor of Molecular Biophysics and Biochemistry and of Physics

Research Interests

Protein-Protein Interactions; Disordered Proteins; Protein Aggregation; Protein Folding; Fluorescence Spectroscopy


Research Summary

The research in my lab focuses on proteins whose aggregation is associated with two age-related neurodegenerative disorders, Alzheimer's and Parkinson's diseases. We study the proteins in the context of trying to understand both their native functions, as well as the factors that contribute to their misfunction in disease. The techniques we use primarily are single molecule fluorescence and associated time-resolved fluorescence methods, including fluorescence correlation spectroscopy and fluorescence lifetime measurements. Currently, much of our work is in reconstituted model systems, but efforts are underway to translate some of our work into cellular models. We collaborate with several groups both at Yale and at other universities who are working on computational and theoretical approaches that complement our experiments.

Extensive Research Description

The research in my lab focuses on proteins whose aggregation is associated with two age-related neurodegenerative disorders, Alzheimer's and Parkinson's diseases. We study the proteins in the context of trying to understand both their native functions, as well as the factors that contribute to their misfunction in disease. The techniques we use primarily are single molecule fluorescence and associated time-resolved fluorescence methods, including fluorescence correlation spectroscopy and fluorescence lifetime measurements. Currently, much of our work is in very simple, reconstituted model systems, but efforts are underway to translate some of our work into cellular models. We collaborate with several groups both at Yale and at other universities who are working on computational and theoretical approaches that complement our experiments.


Selected Publications

  • S. Elbaum-Garfinkle and E. Rhoades, “Long-Range Interactions Modulate Aggregation of Tau by Altering the Conformational Ensemble” in press at Journal of the American Chemical Society September 2012
  • A. Nath, M. Sammalkorpi, D. DeWitt, A.J. Trexler, S. Elbaum-Garfinkle, C.S. O’Hern and E. Rhoades, “The Conformational Ensembles of a-Synuclein and Tau: Combining Single-Molecule FRET and Simulations” in press at Biophysical Journal September 2012
  • V. Ducas and E. Rhoades, “Quantifying ß-Synuclein and ?-Synuclein Membrane Interactions” in press at Journal of Molecular Biology August 2012
  • A. Nath, A. D. Miranker, and E. Rhoades (2011) “A Membrane-bound Dimer of Islet Amyloid Polypeptide Studied by Single-Particle FRET” Angewandte Chemie, 50: 10859-10862
  • N.B. Last, E. Rhoades, and A.D. Miranker (2011) “Islet Amyloid Polypeptide Demonstrates A Persistent Capacity to Disrupt Membrane Integrity” Proceedings of the National Academy of Sciences, U.S.A., 108: 9460-9465
  • E. Sevcsik, A.J. Trexler, J.M. Dunn, and E. Rhoades (2011) “Allostery in a disordered protein: Oxidative modifications to a-Synuclein act distally to regulate membrane binding” Journal of the American Chemical Society, 133: 7152-7158
  • A. J. Trexler and E. Rhoades “a-Synuclein binds large unilamellar vesicles as an extended helix” Biochemistry, 48, (2009) 2304-2306
  • H. Chen and E. Rhoades, “Fluorescence Characterization of Denatured Proteins” Current Opinions in Structural Biology, 18, (2008) 516-524

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