研究领域
Physical/Analytical/Biochemistry/Chemical Physics
Biophysical Chemistry, NMR Spectroscopy, Protein Structure & Dynamics, Molecular Self-Assembly
Our research is focused on the development of multidimensional magic-angle spinning solid-state NMR techniques, and their application to the detailed analysis of 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
• Characterization of chromatin structure and dynamics
• Structural analysis of biologically-inspired synthetic nanomaterials
• 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, Eli Lilly and the Evans Disease Endowment Fund at Ohio State.
Dr. Jaroniec will be taking graduate students this year and welcomes inquiries about openings in his group.
近期论文
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C.P. Jaroniec, Structural studies of proteins by paramagnetic solid-state NMR spectroscopy, J. Magn. Reson. 2015, in press.
T.F. Cunningham, M.D. Shannon, M.R. Putterman, R.J. Arachchige, I. Sengupta, M. Gao, C.P. Jaroniec, S. Saxena, Cysteine specific Cu2+ chelating tags used as paramagnetic probes in double electron electron resonance, J. Phys. Chem. B 2015, 119, 2839-2843.
I. Sengupta, M. Gao, R.J. Arachchige, P.S. Nadaud, T.F. Cunningham, S. Saxena, C.D. Schwieters, C.P. Jaroniec, Protein structural studies by paramagnetic solid-state NMR spectroscopy aided by a compact cyclen-type Cu(II) binding tag, J. Biomol. NMR 2015, 61, 1-6.
G.T. Debelouchina, M.J. Bayro, A.W. Fitzpatrick, V. Ladizhansky, M.T. Colvin, M.A. Caporini, C.P. Jaroniec, V.S. Bajaj, M. Rosay, C.E. MacPhee, M. Vendruscolo, W.E. Maas, C.M. Dobson, R.G. Griffin, Higher order amyloid fibril structure by MAS NMR and DNP spectroscopy, J. Am. Chem. Soc. 2013, 135, 19237-19247.
M. Gao, P.S. Nadaud, M.W. Bernier, J.A. North, P.C. Hammel, M.G. Poirier, C.P. Jaroniec, Histone H3 and H4 N-terminal tails in nucleosome arrays at cellular concentrations probed by magic angle spinning NMR spectroscopy, J. Am. Chem. Soc. 2013, 135, 15278-15281.
I. Sengupta, P.S. Nadaud, C.P. Jaroniec, Protein structure determination with paramagnetic solid-state NMR spectroscopy, Acc. Chem. Res. 2013, 46, 2117-2126.
J.J. Helmus, C.P. Jaroniec, Nmrglue: An open source Python package for the analysis of multidimensional NMR data, J. Biomol. NMR 2013, 55, 355-367.
A.W.P. Fitzpatrick, G.T. Debelouchina, M.J. Bayro, D.K. Clare, M.A. Caporini, V.S. Bajaj, C.P. Jaroniec, L. Wang, V. Ladizhansky, S.A. Muller, C.E. MacPhee, C.A. Waudby, H.R. Mott, A. De Simone, T.P.J. Knowles, H.R. Saibil, M. Vendruscolo, E.V. Orlova, R.G. Griffin, C.M. Dobson, Atomic structure and hierarchical assembly of a cross-β amyloid fibril, Proc. Natl. Acad. Sci. USA 2013, 110, 5468-5473.
T.F. Cunningham, M.S. McGoff, I. Sengupta, C.P. Jaroniec, W.S. Horne, S. Saxena, High-resolution structure of a protein spin-label in a solvent-exposed β-sheet and comparison with DEER spectroscopy, Biochemistry 2012, 51, 6350-6359.
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.
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.
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.
H. Shao, M. Gao, S.H. Kim, C.P. Jaroniec, J.R. Parquette, Aqueous self-assembly of L-lysine based amphiphiles into 1D n-type nanotubes, Chem. Eur. J. 2011, 17, 12882-12885.
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.
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.
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.
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.
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.
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.
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.