E. James Petersson
Assistant Professor of Chemistry

Research

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

• 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 Publications

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

Office Location

350 N

Phone

215-746-2221

Department of Chemistry

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

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