Christopher Jaroniec received his B.S. degree in Chemistry from Kent State University in 1997, his Ph.D. in Physical Chemistry from the Massachusetts Institute of Technology in 2003, where he was a National Science Foundation Graduate Research Fellow with Robert Griffin, and was a Damon Runyon Cancer Research Foundation Postdoctoral Fellow with Ad Bax at the National Institutes of Health. He joined the chemistry faculty at The Ohio State University in 2006, and was promoted to Associate Professor in 2011. Professor Jaroniec has received a CAREER award from the National Science Foundation, an Eli Lilly Young Investigator Award in Analytical Chemistry and a Camille Dreyfus Teacher-Scholar Award.

Our research is focused primarily on the development of advanced multidimensional magic-angle spinning solid-state NMR techniques, and their application to the detailed analysis of the molecular structure, conformational dynamics and intermolecular interactions of otherwise intractable biological macromolecules that are of fundamental importance to human health. We also develop and apply multidimensional solution-state NMR methods and employ computational, biophysical, biochemical and molecular biology approaches for certain aspects of our work. Current research directions include:
• Development of solid-state NMR methods for probing long range structure in proteins via the incorporation of covalently-bound paramagnetic tags
• Design of NMR pulse sequences for site-resolved measurement of structural and dynamic data in proteins with improved precision and accuracy
• Elucidation of the structural basis of protein conformational inheritance in amyloid and prion diseases
• Elucidation of the molecular level interactions between small molecule ligands and supramolecular amyloid peptide and protein assemblies

Our work is currently funded by the National Science Foundation, the National Institutes of Health, the Camille & Henry Dreyfus Foundation, and Eli Lilly.

Dr. Jaroniec will be taking graduate students this year and welcomes inquiries about openings in his group.

Selected publications (the complete publication list is available on our research group's web page)

C.P. Jaroniec, Solid-state nuclear magnetic resonance structural studies of proteins using paramagnetic probes, Solid State Nucl. Magn. Reson. 2012, 43-44, 1-13. doi: 10.1016/j.ssnmr.2012.02.007

I. Sengupta, P.S. Nadaud, J.J. Helmus, C.D. Schwieters, C.P. Jaroniec, Protein fold determined by paramagnetic magic-angle spinning solid-state NMR spectroscopy, Nature Chem. 2012, 4, 410-417. doi: 10.1038/nchem.1299

E.M. Jones, B. Wu, K. Surewicz, P.S. Nadaud, J.J. Helmus, S. Chen, C.P. Jaroniec, W.K. Surewicz, Structural polymorphism in amyloids: New insights from studies with Y145Stop prion protein fibrils, J. Biol. Chem. 2011, 286, 42777-42784. doi: 10.1074/jbc.M111.302539

J.J. Helmus, K. Surewicz, M.I. Apostol, W.K. Surewicz, C.P. Jaroniec, Intermolecular alignment in Y145Stop human prion protein amyloid fibrils probed by solid-state NMR spectroscopy, J. Am. Chem. Soc. 2011, 133, 13934-13937. doi: 10.1021/ja206469q

P.S. Nadaud, I. Sengupta, J.J. Helmus, C.P. Jaroniec, Evaluation of the influence of intermolecular electron-nucleus couplings and intrinsic metal binding sites on the measurement of ¹⁵N longitudinal paramagnetic relaxation enhancements in proteins by solid-state NMR, J. Biomol. NMR 2011, 51, 293-302. doi: 10.1007/s10858-011-9536-y

S. Mukherjee, S.P. Pondaven, C.P. Jaroniec, Conformational flexibility of a human immunoglobulin light chain variable domain by relaxation dispersion nuclear magnetic resonance spectroscopy: Implications for protein misfolding and amyloid assembly, Biochemistry 2011, 50, 5845-5857. doi: 10.1021/bi200410c

P.S. Nadaud, J.J. Helmus, I. Sengupta, C.P. Jaroniec, Rapid acquisition of multidimensional solid-state NMR spectra of proteins facilitated by covalently bound paramagnetic tags, J. Am. Chem. Soc. 2010, 132, 9561-9563. doi: 10.1021/ja103545e

H. Shao, J. Seifert, N.C. Romano, M. Gao, J.J. Helmus, C.P. Jaroniec, D.A. Modarelli, J.R. Parquette, Amphiphilic self-assembly of an n-type nanotube, Angew. Chem. Int. Ed. 2010, 49, 7688-7691. doi: 10.1002/anie.201003415

J.J. Helmus, K. Surewicz, W.K. Surewicz, C.P. Jaroniec, Conformational flexibility of Y145Stop human prion protein amyloid fibrils probed by solid-state nuclear magnetic resonance spectroscopy, J. Am. Chem. Soc. 2010, 132, 2393-2403. doi: 10.1021/ja909827v

I. Jedidi, F. Zhang, H. Qiu, S.J. Stahl, I. Palmer, J.D. Kaufman, P.S. Nadaud, S. Mukherjee, P.T. Wingfield, C.P. Jaroniec, A.G. Hinnebusch, Activator Gcn4 employs multiple segments of Med15/Gal11, including the KIX domain, to recruit Mediator to target genes in vivo, J. Biol. Chem. 2010, 285, 2438-2455. doi: 10.1074/jbc.M109.071589

P.S. Nadaud, J.J. Helmus, S.L. Kall, C.P. Jaroniec, Paramagnetic ions enable tuning of nuclear relaxation rates and provide long-range structural restraints in solid-state NMR of proteins, J. Am. Chem. Soc. 2009, 131, 8108-8120. doi: 10.1021/ja900224z

J.J. Helmus, K. Surewicz, P.S. Nadaud, W.K. Surewicz, C.P. Jaroniec, Molecular conformation and dynamics of the Y145Stop variant of human prion protein in amyloid fibrils, Proc. Natl. Acad. Sci. USA 2008, 105, 6284-6289. doi: 10.1073/pnas.0711716105

J.J. Helmus, P.S. Nadaud, N. Höfer, C.P. Jaroniec, Determination of methyl ¹³C-¹⁵N dipolar couplings in peptides and proteins by three-dimensional and four-dimensional magic-angle spinning solid-state NMR spectroscopy, J. Chem. Phys. 2008, 128, 052314. doi: 10.1063/1.2817638

P.S. Nadaud, J.J. Helmus, N. Höfer, C.P. Jaroniec, Long-range structural restraints in spin-labeled proteins probed by solid-state nuclear magnetic resonance spectroscopy, J. Am. Chem. Soc. 2007, 129, 7502-7503. doi: 10.1021/ja072349t