Our research is at the interface of molecular biophysics, chemical biology, and synthetic biology. The group has two main intertwined goals: We want to understand how proteins fold and assemble into complex assemblies in their native cellular context, and to exploit the protein synthesis machinery to direct the construction of novel protein-based materials. In the long term, we hope to apply our discoveries to better understand protein-based human diseases and enable sustainable alternatives to plastics and other consumer materials.
Sydney Brenner asserted, "Progress in science depends on new techniques, new discoveries, and new ideas – probably in that order." In keeping with that spirit, to make progress on these challenging fronts, we synthesize new molecular probes, engineer new organisms, and develop new mass spec methods.
Protein Folding in vivo
We want to watch proteins inside cells to understand how physics and biology work together to build the world’s most proficient catalysts and molecular machines.
Cross-linking mass-spectrometry enables molecular interactions to be captured in situ. As an emerging tool, we develop new methods and molecules toward the goal of studying biophysical phenomena in living cells.
We are building a “loopable translator” which can iterate over mRNA sequences like a for loop in order to enable living assembly of programmable, hierarchical protein materials.
Novel Fibrous Proteins
Engineering and evolving new fibrous proteins to offer sustainable alternatives to plastics, concrete, and other consumer materials.
Recent News and Publications
Our Q-Exactive HF-X has cleared customs and arrived safely in Remsen in four massive boxes!
We are grateful and excited that Hopkins is supporting our lab with its own orbitrap mass spectrometer!
Potential future graduate students interested in our projects will have the chance to learn more about our research group then.
Boxer, S. G.; Fried, S. D.; Schneider, S. H.; Wu, Y. Proceedings of the 24th International Solvay Conference on Chemistry, World Scientific Publishing Co. 2017, 274-279.
Proton Network Flexibility Enables Robustness and Large Electric Fields in the Ketosteroid Isomerase Active Site
Wang, L.; Fried, S. D.; Markland, T. E. J. Phys. Chem. B, 2017, 121, 9807–9815. [DOI]
The Chemistry Department is pleased to announce that Dr. Stephen Fried will join the faculty as an Assistant Professor, starting in the summer of 2018.
Elliott, T. S.; Biano, A.; Townsley, F. M.; Fried, S. D.; Chin, J. W. Cell Chem. Biol. 2016, 23, 805-815. [DOI]
Wu, Y.; Fried, S. D.; Boxer, S. G. Biochemistry 2015, 54, 7110–7119. [DOI]
Response to Comments on ‘Extreme electric fields power catalysis in the activesite of ketosteroid isomerase.’
Fried, S. D.; Boxer, S. G. Science 2015, 349, 936. [DOI]
Fried, S. D.; Schmied, W. H.; Uttamapinant, C.; Chin, J. W. Angew. Chem. Int. Ed. 2015, 54, 12791–12794. [DOI]
Fried, S. D.; Boxer, S. G. Acc. Chem. Res. 2015, 48, 998-1006. [DOI]
Fried, S. D.; Bagchi, S.; Boxer, S. G. Science 2014, 346, 1510-1514. [DOI]
Wang, L.; Fried, S. D.; Boxer, S. G.; Markland, T. M. Proc. Natl. Acad. Sci. USA 2014, 111, 18454–18459. [DOI]
Mu, X.; Wang, Q.; Wang, L.-P.; Fried, S. D.; Piquemal, J.-P.; Dalby, K. N.; Ren, P. J. Phys. Chem. B 2014, 118, 6456-6465. [DOI]
Fried, S. D.; Wang, L.-P.; Boxer, S. G.; Ren, P.; Pande, V. S. J. Phys. Chem. B 2013, 117, 16236–16248. [DOI]
Measuring Electrostatic Fields in Both Hydrogen Bonding and non-Hydrogen Bonding Environments Using Carbonyl Vibrational Probes
Fried, S. D.; Bagchi, S.; Boxer, S. G. J. Am. Chem. Soc. 2013, 135, 11181-11192. [DOI]
Fried, S. D.; Boxer, S. G. Proc. Natl. Acad. Sci. USA 2013, 110, 12271-12276. [DOI]
Quantitative Dissection of Hydrogen Bond-Mediated Proton Transfer in the Ketosteroid Isomerase Active Site
Sigala, P. A.; Fafarman, A. T.; Schwans, J.P.; Fried, S. D.; Fenn, T. D.; Caaveiro, J. M. M.; Pybus, B.; Ringe, D.; Petsko, G. A.; Boxer, S. G.; Herschlag, D. Proc. Natl. Acad. Sci. USA 2013, 110, E2552-E2561. [DOI]
Bagchi, S.; Fried, S. D.; Boxer, S. G. J. Am. Chem. Soc. 2012, 134, 10373-10376. [DOI]
Solvent-induced Infrared Frequency Shifts in Aromatic Nitriles are Quantitatively Described by the Vibrational Stark Effect
Levinson, N. M.; Fried, S. D.; Boxer, S. G. J. Phys. Chem. B 2012, 116, 10470-10476. (Rich Mathies festschrift) [DOI]
Evaluation of the Energetics of the Concerted Acid-Base Mechanism in Enzymatic Catalysis: The Case of Ketosteroid Isomerase
Fried, S. D.; Boxer, S. G. J. Phys. Chem. B 2012, 116, 690-697. [DOI]
Rosenthal, J.; Chng, L. L.; Fried, S. D.; Nocera, D. G. Chem. Commun. 2007, 25, 2642-2644. [DOI]