Biological

Biological Chemistry seminar, Aaron Esser-Kahn, UC Irvine

Thu, 2014-09-11 15:00 - 16:00
Location: 
Carolyn Hoff Lynch Room

Special Seminar: Andrew Lee (Northwestern)

Tue, 2014-07-08 15:30 - 16:30
Speaker: 
Dr. Andrew Lee Northwestern University
Location: 
Lynch Lecture Hall
Attached Document: 
Interaction of Nanoparticle-Oligonucleotide Conjugates with Serum Nucleases

Joachim Frank Sympsoium

Wed, 2014-04-23 08:30 - 15:00
Speaker: 

The Ribosome: Structure and Function

 

Research Symposium Honoring 2014 Franklin Medal Laureate Joachim Frank

Location: 

Smilow Center for Translational Research

Attached Document: 

Speakers

 

Peter B. Moore, Ph.D.

Sterling Professor of Chemistry, Professor of Molecular Biophysics and Biochemistry, Yale University

 

Barry S. Cooperman, Ph.D.

Professor of Chemistry and Biological Chemistry, University of Pennsylvania

 

Christian Spahn, Ph.D.

Director, Institute for Medical Physics and Biophysics, Charité-Universitätsmedizin, Berlin

 

Yifan Cheng, Ph.D.

Research Professor of Biochemistry and Biophysics, University of California San Francisco

Elizabeth Rhoades

Photo: 
First Name: 
Elizabeth
Last Name: 
Rhoades
Official Title: 
Associate Professor of Chemistry
Contact Information
Office Location: 
258 Chemistry Building
Email: 
elizabeth.rhoades@sas.upenn.edu
Phone: 
215-573-6477
Fax: 
215-573-2112
Admin Support: 
Education: 
  • postdoctoral associate with Professor Watt Webb at Cornell University (2003-2006)
  • postdoctoral associate with Professor Gilad Haran at the Weizmann Institute of Science (2001-2003)
  • PhD in Biophysics from the University of Michigan, Ann Arbor (2001)
  • B.S. in Physics from Duke University (1994)
Research Interests: 

Research in the Rhoades lab aims to elucidate the principles that link protein conformational change with structure-function relationships, focusing on understanding structural plasticity in intrinsically disordered proteins (IDPs). IDPs do not form stable structures under physiological conditions; for many, function is dependent upon disorder. This is in striking contrast to the structure-function paradigm that dominates our understanding of globular proteins. Given the large fraction of the eukaryotic proteome predicted to be disordered, the scope of the problem and the need for new insights are enormous.

 

Much of our effort is directed towards IDPs whose aggregation is central to the pathology of several degenerative diseases: α-synuclein (Parkinson’s disease), tau (Alzheimer’s disease), and IAPP (Type II Diabetes). These three proteins have diverse native functions and binding partners, but share intriguing commonalities of toxic mechanism and the importance of templated selfassembly. Studying systems in parallel allows us to generate protein and disease-specific insights as well as determine principles relevant to general functional and dysfunctional mechanisms of IDPs.

 

Our primary approaches center on single molecule optical techniques. These approaches enable quantitative and structural assessments of our systems in isolation and in the context of biologically relevant interactions. Single molecule approaches are unique in their ability to characterize systems which exist and function as a dynamic ensemble of states.

Selected Publications: 

1.      X.-H. Li, J. A. Culver, and E. Rhoades (2015) “Tau binds to multiple tubulin dimers with helical structure” Journal of the American Chemical Society, 137: 9218-921


2.     A. Nath, D. E. Schlamadinger, E. Rhoades, and A.D. Miranker (2015) “Structure-based small molecule modulation of a pre-amyloid state: pharmacological enhancement of IAPP membrane-binding and toxicity” Biochemistry, 349: 54-58

3.     D. Jülich, G. Cobb,  A.M. Melo, P. McMillen, A. Lawton,  S.G.J. Mochrie, E. Rhoades, and S.A. Holley (2015) “Cross-scale Integrin regulation organizes ECM and tissue topology” Developmental Cell, 34: 33-44

4.     J. LaRochelle, G. Cobb, A. Steinauer, E. Rhoades, and A. Schepartz (2015) “Fluorescence correlation spectroscopy revealsy highly efficient endosomal escape by certain penta-arg proteins and stapled peptides” Journal of the American Chemical Society. 127: 2536-2541 January 2015

5.     S.Kumar, D.E. Schlamadinger, M.A. Brown, J.M. Dunn, B. Mercado, J.A. Hebda, I Saraogi, E. Rhoades, A.D. Hamilton, and A.D. Miranker (2014) “IAPP and the shared molecular origins of leakage and toxicity” Chemistry and Biology, 19: 369-378

6.     A.R. Braun, M.M. Lacy, V.C. Ducas, E. Rhoades, and J.N. Sachs (2014) “α-Synuclein-induced membrane remodeling is driven by binding affinity, partition depth, and interleaflet order asymmetry” Journal of the American Chemical Society, 136: 9962-9972

7.  S. Elbaum-Garfinkle, G. Cobb, J. T. Compton, X. Li and E. Rhoades (2014)“Tau mutants bind tubulin heterodimers with enhanced affinity” Proceedings of the National Academy of Sciences U.S.A., 111: 6311-6316

8.  D. C. DeWitt and E. Rhoades (2013) “α-Synuclein Inhibits SNARE-mediated Vesicle Fusion Through Direct Interactions with Lipid Bilayer” Biochemistry, 52: 2385-2387

9.  B. R. Capraro, Z. Shi, J.M. Dunn, T. Wu, E. Rhoades, and T. Baumgart (2013) “Kinetics of endophilin N-BAR domain dimerization and membrane interactions” Journal of Biological Chemistry, 288: 12533-12543

10.  S. Elbaum-Garfinkle and E. Rhoades (2012) “Long-Range Interactions Modulate Aggregation of Tau by Altering the Conformational Ensemble” Journal of the American Chemical Society, 134: 16607-16613

11.     A. Nath, M. Sammalkorpi, D. DeWitt, A.J. Trexler, S. Elbaum-Garfinkle, C.S. O’Hern and  E. Rhoades (2012) “The Conformational Ensembles of  α-Synuclein and Tau:  Combining Single-Molecule FRET and Simulations”  Biophysical Journal, 103: 1940-1949

12.     V. Ducas and E. Rhoades (2012) “Quantifying β-Synuclein and g-Synuclein Membrane Interactions”  Journal of Molecular Biology, 423:528-539

13.     A.J. Trexler and E. Rhoades  (2012) “N-terminal acetylation is critical for forming α-helical oligomer of α-Synuclein” Protein Science, 21:601-605  

14.     A.R. Braun, E. Sevcsik, P. Chin, E. Rhoades, S. Tristram-Nagle, and J.N. Sachs (2012) “α-Synuclein Induces Both Positive Mean Curvature and Negative Gaussian Curvature in Membranes” Journal of the American Chemical Society,  134: 2613-2620  

15.     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   
   
16.     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   

17.     E. Sevcsik, A.J. Trexler, J.M. Dunn, and E. Rhoades (2011) “Allostery in a disordered protein: Oxidative modifications to α-Synuclein act distally to regulate membrane binding” Journal of the American Chemical Society, 133: 7152-7158  

18.  A.J. Trexler and E. Rhoades (2010) “Single molecule characterization of α-Synuclein in aggregation-prone states” Biophysical Journal, 99: 3048-3055    

19.  E. R. Middleton and E. Rhoades (2010) “Effects of vesicle curvature and composition on α-Synuclein binding to lipid vesicles” Biophysical Journal, 99: 2279-2288  

20.  A . J. Trexler and E. Rhoades (2009) “α-Synuclein binds large unilamellar vesicles as an extended helix”Biochemistry, 48: 2304-2306  

Special Biological Seminar: Joshua Rabinowitz, Princeton University

Thu, 2014-03-13 10:30 - 11:30
Speaker: 

Prof. Joshua D. Rabinowitz

Princeton University

Location: 

Lynch Lecture Hall

Attached Document: 

Towards a Comprehensive Understanding of Cellular Metabolism

 

For more information on Prof. Rabinowitz, please visit here.

Special Energy Seminar: L. Robert Baker, Berkeley

Tue, 2013-11-26 22:00
Speaker: 

Dr. L. Robert Baker   
University of California, Berkeley

Location: 

Carolyn Hoff Lynch Lecture Hall
Chemistry Complex
231 South 34th Street

Attached Document: 

Charge Transfer and Chemistry at Catalytic Interfaces

Abstract

Department of Chemistry

231 S. 34 Street, Philadelphia, PA 19104-6323

215.898.8317 voice | 215.573.2112 fax | web@chem.upenn.edu

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