E. James Petersson
Assistant Professor of Chemistry
Office: 350 N
Research Group Website: http://ejpweb1.chem.upenn.edu
Protein motion underlies both proper function and disease in biological systems. Many signaling and transport proteins require complex rearrangements for function, and some proteins, such as amyloids, misfold into toxic conformations. Studying these protein motions not only aids our understanding of diverse biological phenomena, it also contributes to an important fundamental problem in biochemistry: understanding how motions propagate from one end of a protein to another. The Petersson laboratory is developing tools to address questions of how dynamic proteins mediate communication and how the cellular environment catalyzes protein misfolding, from detailed in vitro folding studies to modeling protein motion in living cells. These tools include novel chromophores, which we synthesize and incorporate into proteins through unnatural amino acid mutagenesis and synthetic protein ligation.
Education and Academic History
- B.A. Dartmouth College (1998)
- Ph.D. California Institute of Technology (2005)
- NIH/NINDS Predoctoral Fellow (2004-2005)
- NIH/NIGMS Postdoctoral Fellow, Yale University (2006-2008)
- Searle Scholar (2010)
- Sloan Research Fellow (2012)
- NSF CAREER Award (2012)
Selected PublicationsFrom University of Pennsylvania
Native Chemical Ligation of Thioamide-Containing Peptides: Development and Application to the
Synthesis of Labeled α-Synuclein for Misfolding Studies
Batjargal, S.; Wang, Y. J.; Goldberg, J. M. Wissner, R. F.; Petersson, E. J.
J. Am. Chem. Soc. 2012, 134, 9172-9182.
Highlighted in C&E News and selected for the cover of JACS.
Minimalist Chromophores to Monitor Protein Dynamics: Thioamide Quenching of Selectively-Excitable Fluorescent Amino Acids
Goldberg, J. M.; Speight, L. C.; Fegley, M. W.; Petersson, E. J.
J. Am. Chem. Soc. 2012, 134, 6088-6091.
Highlighted in C&E News.
Thioamide Quenching of Intrinsic Protein Fluorescence
Goldberg, J. M.; Wissner, R. F.; Klein, A. M.; Petersson, E. J.
Chem. Commun. 2012, 48, 1550-1552.
Included in ChemComm Emerging Investigator Issue.
A Simple Chemoenzymatic Method for N-Terminal Protein Modification
Wagner, A. M.; Fegley, M. W.; Warner, J. B.; Grindley, C. L. J.; Marotta, N. P.; Petersson, E. J.
J. Am. Chem. Soc. 2011, 133, 15139-15147.
Thioamides as Fluorescence Quenching Probes: Minimalist Chromophores to Monitor Protein Dynamics
Goldberg, J. M.; Batjargal, S.; Petersson, E. J.
J. Am. Chem. Soc. 2010, 132, 14718-14720.
From Yale University
Petersson, E. J.; Schepartz, A. “Toward â-Amino Acid Proteins: Design, Synthesis, and Characterization of a 15-Kilodalton â-Peptide Tetramer” J. Am. Chem. Soc. 2008, 120, 821-823.
Daniels, D. S.; Petersson, E. J.; Qiu, J.; Schepartz, A. “High Resolution Structure of a â-Peptide Bundle” J. Am. Chem. Soc. 2007, 129, 1532-1533.
Selected as one of the “Highlights of 2007” by Chemical and Engineering News. Also featured in HHMI News Bulletin, MIT’s Technology Review, Biomedical Beat, DrugResearcher.com, and Chemistry World.
McMenimen, K. A.; Petersson, E. J.; Lester, H. A.; Dougherty D. A. “Probing the Mg2+ Blockade Site of the NMDA Receptor with Unnatural Amino Acid Mutagenesis” ACS Chem. Biol. 2006, 1, 227-234.
Cashin, A. L.; Petersson, E. J.; Lester, H. A.; Dougherty, D. A. “Using Physical Chemistry to Differentiate Nicotinic from Cholinergic Agonists at the Nicotinic Acetylcholine Receptor“ J. Am. Chem. Soc. 2005, 127, 350-356.