2014 NOBCChE Lecture

Thu, 2014-05-01 16:00 - 17:00
Speaker: 

Prof. John A.W. Harkless

Howard University

Location: 

Lynch Lecture Hall

Attached Document: 

The Research Life of a Minority Chemist: How a Difference in Perspective Aids Chemical Intuition

 

Jessica M. Anna

Photo: 
First Name: 
Jessica M.
Last Name: 
Anna
Official Title: 
Assistant Professor of Chemistry

Physical Chemistry, Laser Spectroscopy, Ultrafast Dynamics, Chemical Reaction Dynamics, and Energy Science

Additional Titles: 
Elliman Faculty Fellow
Contact Information
Office Location: 
251 Chem
Email: 
jmanna@sas.upenn.edu
Phone: 
215-746-2354
Admin Support: 
Education: 

B.S. University of Pittsburgh (2006)

 

Ph.D. University of Michigan (2011)

 

Postdoctoral Research Fellow, University of Michigan (2011)

 

Postdoctoral Research Fellow, University of Toronto (2011-2014)

Research Interests: 

Solar energy conversion, in both natural and artificial systems, involves the absorption of a photon that can then lead to a series of energy and electron transfer events. Research in the Anna group focuses on understanding these photoinitiated processes. More specifically we are interested in exploring (1) the interplay of vibrational motion with both electronic energy transfer and electron transfer reactions, and (2) the role the environment plays in these processes. To begin to answer these questions we employ both well-established and novel multidimensional spectroscopic techniques to explore photoinitiated processes in a range of systems, spanning interests in biology, chemistry, and physics.

Selected Publications: 

J. M. Anna, M. R. Ross, K. J. Kubarych, “Dissecting Enthalpic and Entropic Barriers to Ultrafast Equilibrium Isomerization of a Flexible Molecule Using 2DIR Chemical Exchange Spectroscopy”, J. Phys. Chem. A 113 (2009) 6544-6547.

 

J. M. Anna and K. J. Kubarych, “Watching Solvent Friction Impede Ultrafast Barrier Crossings: A Direct Test of Kramers Theory”, J. Chem. Phys. 133 (2010) 174596.

 

J. M. Anna, M. J. Nee, C. R. Baiz, R. McCanne, K. J. Kubarych, “Measuring Absorptive Two-Dimensional Infrared Spectra Using Chirped-Pulse Upconversion Detection”, J. Opt. Soc. Am. B. 27 (2010) 382-393.

 

J. M. Anna, E. E. Ostroumov, K. Maghlaoui, J. Barber, and G. D. Scholes “Two-Dimensional Electronic Spectroscopy Reveals Ultrafast Downhill Energy Transfer in Photosystem I Trimers of the Cyanobacterium Thermosynechococcus elongatus”, J. Phys. Chem. Lett. (2012), 3, 3677-3684.

 

J. M. Anna, Y. Song, R. Dinshaw and G. D. Scholes “Two-dimensional electronic spectroscopy for mapping photophysics”, Pure. Appl. Chem. (2013), 85, 1307-1319.

 

J. M. Anna, G. D. Scholes, and R. van Grondelle, “A Little Coherence in Photosynthetic Light Harvesting”, BioScience (2014), 64, 14-25

Penn Chemistry hires Jessica Anna

Dr. Jessica Anna, currently a postdoctoral fellow at the University of Toronto, will join the department as an assistant professor on July 1, 2014. Dr. Anna is the first hire in the School of Arts & Sciences' Energy Cluster program in the natural sciences.

 

Timothy J Deming, University of California, Special Bioengineering, Chemistry and Biochem. Seminar

Thu, 2014-04-10 12:00 - 13:30
Location: 

 

337 Towne Building

 

Title: "Synthetic Polypeptide Materials for Biomedical Applications"

 

Marsha Lester and Larry Sneddon honored in Dallas

Marsha I. Lester, the Edmund J. Kahn Distinguished Professor, and Larry G. Sneddon, the Blanchard Professort of Chemistry, were both honored with national awards at the ACS meeting. Marsha was awarded the Francis P. Garvan-John M. Olin Medal, which recognizes distinguished service to chemistry by women chemists. Larry received the F. Albert Cotton Award, which was established to recognize distinguished work in synthetic inorganic chemistry. Both Marsha and Larry were honored at the awards banquet in Dallas.

 

Penn Chemistry adds two new faculty members for 2015

Associate Professor Elizabeth Rhoades (Yale) will be joining the Department in July 2015. The Rhoades lab studies protein folding, misfolding, and dynamics.

 

Neil S. Tomson, currently at Los Alamos National Laboratory, will join the Department at the same time as an Assistant Professor of Inorganic Chemistry.

 

We are thrilled to be able to welcome Liz and Neil to Penn Chemistry.

Eric Schelter's Research Featured at Science on Tap

Assistant Professor Eric Schelter brought chemistry to the people when he took part in Philadelphia's Science on Tap series at National Mechanics. Interested members of the general public were on hand to enjoy food, drink, and a spirited conversation about the important, yet little discussed, topic of rare earch metals.

 

Neil C. Tomson

Photo: 
First Name: 
Neil C.
Last Name: 
Tomson
Official Title: 
Assistant Professor of Chemistry

Inorganic and Organometallic Synthesis, Energy Storage Chemistry, Materials Chemistry

Contact Information
Office Location: 
3002 IAST
Email: 
tomson@upenn.edu
Phone: 
(215) 898-6208
Fax: 
(215) 573-2112
Admin Support: 
Education: 
  • B.A. in Chemistry, with honors, Grinnell College (2004)
  • Ph.D. in Chemistry, University of California, Berkeley (2009)
  • Post-doctoral Associate, Max Planck Institute for Bioinorganic Chemistry (2009-2011)
  • Adjunct Assistant Professor of Chemistry, College of St. Benedict | St. John’s University (2011-2012)
  • Post-doctoral Associate, Los Alamos National Laboratory (2012-2013)
  • Glenn T. Seaborg Institute Post-doctoral Fellow, Los Alamos National Laboratory (2013)
  • Director’s Post-doctoral Fellow, Los Alamos National Laboratory (2013-2015)
Research Interests: 

Our group performs synthetic inorganic and organometallic chemistry as a way of investigating new concepts in structure, bonding, catalysis, and materials chemistry.  The research involves the use of rigorous air-sensitive synthetic techniques and draws on a wide range of physical methods for characterizing novel compounds. 

 

With a particular interest in energy problems, our work takes advantage of modern concepts in bonding theory to generate materials that can influence how energy from renewable sources is collected, stored, and released.  To do this, we develop both new catalysts for reactions that store energy in chemical bonds and battery materials that can reversibly deliver multiple electrons with minimal energy loss.  Our current areas of focus include:

 

• Understanding the effects of molecular-scale electrostatic fields on electronic structure and reactivity, particularly as they relate to both bioinorganic chemistry and homogeneous catalysis.

 

• Developing molecular cluster compounds that incorporate redox-active ligands as a way of modeling the chemistry occurring on the surfaces of heterogeneous, metallic catalysts.

 

• Generating molecules for use as multi-electron, redox-flow battery materials, especially those that can undergo potential inversion.

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  

Junrong Zheng, Rice University , Physical Chemistry Seminar

Thu, 2014-04-24 13:00 - 14:00
Speaker: 

Junrong Zheng

Location: 

Lynch Lecture Hall

Chemistry Department

Inquiries Please contact Rosa Vargas rvargas@sas.upenn.edu

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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