• Searle Scholar (2010)
• Sloan Research Fellow (2012)
• NSF CAREER Award (2012)
• Award for Early Excellence in Physical Organic Chemistry (2013)
• Institute on Aging Fellow (2014)
• Thieme Chemistry Journal Award (2017)
• Jane Glick Award for Graduate Teaching (2018)
• A.B. Dartmouth College (1998)
• Ph.D. California Institute of Technology (2005)
• NIH Postdoctoral Fellow, Yale University (2005-2008)
Protein folding and protein interactions underlie both proper function and disease in biological systems. Many receptor proteins signal through complex interactions and rearrangements, and some proteins, such as the Parkinson’s Disease protein α-synuclein, 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 proteins fold and change shape. The Petersson laboratory is developing tools to address questions of how peptides and proteins mediate cellular communication and how the cellular environment catalyzes protein misfolding, from detailed in vitrofolding studies to imaging in live animals. These tools include novel chromophores, which we synthesize and incorporate into proteins through unnatural amino acid mutagenesis and synthetic protein ligation. We apply these tools to several key disease areas through collaborations in the Perelman School of Medicine: preventing the acquisition of antibiotic resistance by bacteria, Parkinson’s Disease, and fluorescence-guided cancer surgery. In many cases, the balance between health and disease is governed by post-translational modifications, for which we study the enzymes that install them, both to understand their biological roles and to utilize them in synthetic protein modification. Finally, an area of particular interest in the Petersson laboratory is the introduction of thioamide modifications to the peptide backbone, which can serve as protein folding probes, or stabilizers for improved therapeutic peptides or in vivoimaging reagents.
Minimal Chromophores to Monitor Protein Motions
Efficient Synthesis and In Vivo Incorporation of Acridon-2-ylalanine, a Fluorescent Amino Acid for Lifetime and Förster Resonance Energy Transfer/Luminescence Resonance Energy Transfer Studies
Lee C. Speight, Anand K. Muthusamy, Jacob M. Goldberg, John B. Warner, Rebecca F. Wissner, Taylor S. Willi, Bradley F. Woodman, Ryan A. Mehl, and E. James Petersson
J. Am. Chem. Soc. 13518806-18814 (2013)
Multicolor Protein FRET with Tryptophan, Selective Coumarin-Cysteine Labeling, and Genetic Acridonylalanine Encoding
John J. Ferrie,* Naoya Ieda,* Conor M. Haney, Christopher R. Walters, Itthipol Sungwienwong, Jimin Yoon, and E. James Petersson
Chem. Commun. 5311072-11075 (2017)
Selected as a Hot Article for 2017!
Using a Large Ensemble FRET Library with Multiple Probe Pairs to Drive Monte Carlo Simulations of Disordered α-Synuclein
John J. Ferrie, Conor M. Haney, Jimin Yoon, Buyan Pan, Yi-Chih Lin, Zahra Fakhraai, Elizabeth Rhoades, Abhinav Nath, and E. James Petersson
Biophys. J. 11453-64 (2018)
Featured on the Biophysical Journal website!
Toward a Molecular Understanding of Parkinson's Disease
Site-Specific Fluorescence Polarization for Studying the Disaggregation of α-Synuclein Fibrils by Small Molecules
Conor M. Haney,* Christina L. Cleveland,* Rebecca F. Wissner,* Lily Owei, Jaclyn Robustell, Malcolm J. Daniels, Merve Canyurt, Priscilla Rodriguez, Harry Ischiropoulos, Tobias Baumgart, and E. James Petersson
Selected for the Biochemistry journal cover and highlighted in Biochemistry Newsflash!
Selective imaging of internalized proteopathic α-synuclein seeds in primary neurons reveals mechanistic insight into transmission of synucleinopathies
Richard J. Karpowicz Jr., Conor M. Haney, Tiberiu S. Mihaila, Raizel M. Sandler, E. James Petersson and Virginia M.-Y. Lee
J. Biol. Chem. 29213482-13497 (2017)
Selected an Editor's Pick in J. Biol. Chem and highlighted by Health Medicine Network, Science Newsline, Medical Xpress, Newswise, EurekAlert!, and ALZForum.
Thioamide Modifications of the Protein Backbone
Thioamide Quenching of Fluorescent Probes through Photoinduced Electron Transfer: Mechanistic Studies and Applications
Jacob M. Goldberg, Solongo Batjargal, Benson S. Chen, and E. James Petersson
J. Am. Chem. Soc. 13518651-18658 (2013)
The Effects of Thioamide Backbone Substitution on Protein Stability: A study in α-helical, β-sheet, and polyproline II helical contexts
Christopher R. Walters, D. Miklos Szantai-Kis, Yitao Zhang, Zachary E. Reinert, W. Seth Horne David M. Chenoweth, and E. James Petersson
Chem. Sci. 82868-2877 (2017)
Thioamide Substitution Selectively Modulates Proteolysis and Receptor Activity of Therapeutic Peptide Hormones
Xing Chen, Elizabeth G. Mietlicki-Baase, Taylor M. Barrett, Lauren E. McGrath, Kieran Koch-Laskowski, John J. Ferrie, Matthew R. Hayes, and E. James Petersson
J. Am. Chem. Soc. 13916688–16695 (2017)
Highlighted in Nature!
Post-Translational Modification Enzymology and Applications
Structure and Mechanism of Acetylation by the N-Terminal Dual Enzyme NatA/Naa50 Complex
Sunbin Deng, Robert S. Magin, Xuepeng Wei, Buyan Pan, E. James Petersson, and Ronen Marmorstein
Structure 271057-1070 (2019)
Transferase-Mediated Labeling of Protein N-Termini with Click Chemistry Handles
Anne M. Wagner, John B. Warner, Haviva E. Garrett, Christopher R. Walters, and E. James Petersson
Methods Mol. Biol. 1337109-127 (2015)
*Authors contributed equally.