{"id":25,"date":"2015-03-18T17:00:10","date_gmt":"2015-03-18T21:00:10","guid":{"rendered":"https:\/\/research.cbc.osu.edu\/jaroniec.1\/?page_id=25"},"modified":"2025-08-15T19:15:56","modified_gmt":"2025-08-15T23:15:56","slug":"publications","status":"publish","type":"page","link":"https:\/\/research.cbc.osu.edu\/jaroniec.1\/publications\/","title":{"rendered":"Publications"},"content":{"rendered":"

Google Scholar<\/a><\/strong>\u00a0\u00a0\u00a0\u00a0\u00a0 ResearcherID<\/a><\/strong>\u00a0\u00a0\u00a0\u00a0\u00a0 MyNCBI<\/a><\/strong><\/p>\n

85. B.P. Tatman, V. Sridharan, M. Uttarkabat, C.P. Jaroniec, M. Ernst, P. Rovo, P. Schanda, Bumps on the road: The way to clean relaxation dispersion magic-angle spinning NMR, J. Am. Chem. Soc. <\/i>2025<\/b>, 147<\/i>, 29315\u2013<\/span>29326. [<\/a>pdf<\/a>]<\/a> [<\/a>doi<\/a>]<\/a> [pubmed<\/a>]<\/p>\n

84. V. Sridharan, T. George, D.W. Conroy, Z. Shaffer, W.K. Surewicz, C.P. Jaroniec, Copper binding alters the core structure of amyloid fibrils formed by Y145Stop human prion protein, Phys. Chem. Chem. Phys. <\/i>2024<\/b>, 26<\/i>, 26489\u201326496<\/span>. [<\/a>pdf<\/a>]<\/a> [<\/a>doi<\/a>]<\/a> [pubmed<\/a>]<\/p>\n

83. C.P. Jaroniec, Structural and dynamic studies of chromatin by solid-state NMR spectroscopy, Curr. Opin. Struct. Biol. <\/i>2024<\/b>, 89<\/i>, 102921. [<\/a>pdf<\/a>]<\/a> [<\/a>doi<\/a>]<\/a> [pubmed<\/a>]<\/p>\n

82. R. Muzquiz, C. Jamshidi, D.W. Conroy, C.P. Jaroniec, M.P. Foster, Insights into ligand-mediated activation of an oligomeric ring-shaped gene-regulatory protein from solution and solid-state NMR, J. Mol. Biol. <\/i>2024<\/b>, 436<\/i>, 168792. [<\/a>pdf<\/a>]<\/a> [<\/a>doi<\/a>]<\/a> [pubmed<\/a>]<\/p>\n

81. W. Sun, O.O. Lebedenko, N. Gonzalez Salguero, M.D. Shannon, M. Zandian, M.G. Poirier, N.R. Skrynnikov, C.P. Jaroniec, Conformational and interaction landscape of histone H4 tails in nucleosomes probed by paramagnetic NMR spectroscopy, J. Am. Chem. Soc. <\/i>2023<\/b>, 145<\/span><\/em>, 25478\u201325485<\/span>.<\/span> [<\/a>pdf<\/a>]<\/a> [<\/a>doi<\/a>]<\/a> [pubmed<\/a>]<\/p>\n

80. L. Bhai, J.K. Thomas, D.W. Conroy, Y. Xu, H.M. Al-Hashimi, C.P. Jaroniec, Hydrogen bonding in duplex DNA probed by DNP enhanced solid-state NMR N-H bond length measurements,\u00a0Front. Mol. Biosci.\u00a0<\/i>2023<\/strong>, 10<\/span><\/em>, 1286172.<\/span> [<\/a>pdf<\/a>]<\/a> [<\/a>doi<\/a>]<\/a> [pubmed<\/a>]<\/span><\/p>\n

79. S.T. Smrt, N. Gonzalez Salguero, J.K. Thomas, M. Zandian, M.G. Poirier, C.P. Jaroniec, Histone H3 core domain in chromatin with different DNA linker lengths studied by\u00a01<\/sup>H-detected solid-state NMR spectroscopy,\u00a0Front. Mol. Biosci.\u00a0<\/i>2023<\/strong>, 9<\/span><\/em>, 1106588.<\/span>\u00a0<\/span>[<\/a>pdf<\/a>]<\/a> [<\/a>doi<\/a>]<\/a> [pubmed<\/a>]<\/p>\n

78. Q. Li, C.P. Jaroniec, W.K. Surewicz, Cryo-EM structure of disease-related prion fibrils provides insights into seeding barriers,\u00a0Nat. Struct. Mol. Biol.\u00a0<\/i>2022<\/strong>, 29<\/span><\/em>, 962\u2013965<\/span>.<\/span>\u00a0<\/span>[<\/a>pdf<\/a>]<\/a> [<\/a>doi<\/a>]<\/a> [pubmed<\/a>]<\/p>\n

77. D.W. Conroy, Y. Xu, H. Shi, N. Gonzalez Salguero, R.N. Purusottam, M.D. Shannon, H.M. Al-Hashimi, C.P. Jaroniec, Probing Watson-Crick and Hoogsteen base pairing in duplex DNA using dynamic nuclear polarization solid-state NMR spectroscopy, Proc. Natl. Acad. Sci. USA<\/i> 2022<\/b>,\u00a0119<\/i>, e2200681119. [pdf]<\/a>\u00a0[doi]<\/a> [pubmed]<\/a>
\n\u2022 OSU Research News Article<\/a><\/p>\n

76. Z. Qi, K. Surewicz, W.K. Surewicz, C.P. Jaroniec, Influence of the dynamically disordered N-terminal tail domain on the amyloid core structure of human Y145Stop prion protein fibrils,\u00a0Front. Mol. Biosci.\u00a0<\/i>2022<\/strong>, 9<\/span><\/em>, 841790.<\/span>\u00a0<\/span>[<\/a>pdf<\/a>]<\/a> [<\/a>doi<\/a>]<\/a> [pubmed<\/a>]<\/p>\n

75. M. Zandian, N. Gonzalez Salguero, M.D. Shannon, R.N. Purusottam, T. Theint, M.G. Poirier, C.P. Jaroniec, Conformational dynamics of histone H3 tails in chromatin,\u00a0J. Phys. Chem. Lett.<\/em>\u00a02021<\/strong>, 12<\/span><\/em>, 6174\u20136181. <\/span>[<\/a>pdf<\/a>]<\/a> [<\/a>doi<\/a>]<\/a> [pubmed<\/a>]<\/p>\n

74. S.O.\u00a0Rabdano, M.D. Shannon, S.A. Izmailov, N. Gonzalez Salguero, M. Zandian, R.N. Purusottam, M.G. Poirier, N.R. Skrynnikov, C.P. Jaroniec, Histone H4 tails in nucleosomes: a fuzzy interaction with DNA,\u00a0Angew. Chem. Int. Ed.<\/em>\u00a02021<\/strong>, 60<\/span><\/em>, 6480\u20136487. [<\/a>pdf<\/a>]<\/a> [<\/a>doi<\/a>]<\/a> [pubmed<\/a>]<\/p>\n

73. H.H. Dao, M.Z. Hlaing, Y. Ma, K. Surewicz, W.K. Surewicz, C.P. Jaroniec, 13<\/sup>C and 15<\/sup>N chemical shift assignments of A117V and M129V human Y145Stop prion protein amyloid fibrils,\u00a0Biomol. NMR Assign.<\/em>\u00a02021<\/strong>, 15<\/span><\/em>, 45\u201351. [<\/a>pdf<\/a>]<\/a> [<\/a>doi<\/a>]<\/a> [pubmed<\/a>]<\/p>\n

72. A. Hassan, C.M. Quinn, J. Struppe, I.V. Sergeyev, C. Zhang, C. Guo, B. Runge, T. Theint, H.H. Dao, C.P. Jaroniec, M. Berbon, A. Lends, B. Habenstein, A. Loquet, R. Kuemmerle, B. Perrone, A.M. Gronenborn, T. Polenova, Sensitivity boosts by the CPMAS CryoProbe for challenging biological assemblies, J. Magn. Reson.<\/i> 2020<\/b>, 311<\/span><\/em>, 106680. [pdf<\/a>] [doi]<\/a> [pubmed<\/a>]<\/p>\n

71. S.E. Ashbrook, C.P. Jaroniec, NMR spectroscopy of paramagnetic solids, Solid State Nucl. Magn. Reson.<\/i> 2019<\/b>, 104<\/span><\/em>, 101625. [pdf<\/a>] [doi]<\/a> [pubmed<\/a>]<\/p>\n

70. C.P. Jaroniec, Two decades of progress in structural and dynamic studies of amyloids by solid-state NMR, J. Magn. Reson.<\/i> 2019<\/b>, 306<\/span><\/em>, 42\u201347. [pdf]<\/a> [doi]<\/a> [pubmed<\/a>]<\/p>\n

69.\u00a0A. Perez, K. Gaalswyk, C.P. Jaroniec, J.L. MacCallum,\u00a0High accuracy protein structures from minimal sparse paramagnetic solid-state NMR restraints, Angew. Chem. Int. Ed.<\/i> 2019<\/b>,\u00a058<\/span><\/em>, 6564\u20136568. [pdf<\/a>] [doi<\/a>] [pubmed<\/a>]<\/p>\n

68. D. Aucoin,\u00a0<\/span>Y. Xia<\/span>, T. Theint, P.S. Nadaud, K. Surewicz, W.K. Surewicz, C.P. Jaroniec<\/span>,\u00a0Protein-solvent interfaces in human Y145Stop prion protein amyloid fibrils probed by paramagnetic solid-state NMR spectroscopy, J. Struct. Biol.<\/em>\u00a02019<\/strong>, 206<\/span><\/em>, 36\u201342.\u00a0[pdf<\/a>] [doi<\/a>] [pubmed<\/a>]<\/p>\n

67. M.D. Shannon, T. Theint, D. Mukhopadhyay, K. Surewicz, W.K. Surewicz, D. Marion, P. Schanda,\u00a0C.P. Jaroniec<\/span>, Conformational dynamics in the core of human Y145Stop prion protein amyloid probed by relaxation dispersion NMR, ChemPhysChem<\/em>\u00a02019<\/strong>, 20<\/i>, 311-317. [pdf<\/a>] [doi<\/a>] [pubmed<\/a>]<\/p>\n

66. D. Mukhopadhyay, C. Gupta, T. Theint, C.P. Jaroniec, Peptide bond conformation in peptides and proteins probed by dipolar coupling-chemical shift tensor correlation solid-state NMR, J. Magn. Reson.<\/em> 2018<\/strong>, 297<\/em>, 152\u2013160.\u00a0[pdf<\/a>] [doi<\/a>] [pubmed<\/a>]<\/p>\n

65.\u00a0T. Theint, Y. Xia, P.S. Nadaud, D. Mukhopadhyay, C.D. Schwieters, K. Surewicz, W.K. Surewicz, C.P. Jaroniec, Structural studies of amyloid fibrils by paramagnetic solid-state nuclear magnetic resonance spectroscopy, J. Am. Chem. Soc.<\/em> 2018<\/strong>, 140<\/span><\/em>, 13161\u201313166.\u00a0[pdf<\/a>] [doi<\/a>] [pubmed<\/a>]<\/p>\n

64.\u00a0H. Wang<\/span>, <\/span>Z. Gao<\/span><\/span>, <\/span>X. Liu<\/span>, <\/span>P. Agarwal<\/span>, <\/span>S. Zhao<\/span>, <\/span>D.W. Conroy<\/span>, <\/span>G. Ji<\/span>,\u00a0<\/span>J. Yu<\/span><\/span>,\u00a0<\/span>C.P. Jaroniec<\/span>, <\/span>Z. Liu<\/span>, <\/span>X. Lu<\/span>, <\/span>X. Li,\u00a0<\/span>X. He<\/span>,\u00a0Targeted production of reactive oxygen species in\u00a0<\/span>mitochondria to overcome cancer drug resistance<\/span>, Nat. Commun.<\/em>\u00a02018<\/strong>, 9<\/i>, 562.\u00a0[pdf<\/a>] [doi]<\/a> [pubmed<\/a>]<\/p>\n

63. D. Mukhopadhyay, P.S. Nadaud, M.D. Shannon, C.P. Jaroniec, Rapid quantitative measurements of paramagnetic relaxation enhancements in Cu(II)-tagged proteins by proton-detected solid-state NMR spectroscopy, J. Phys. Chem. Lett.<\/em> 2017<\/strong>, 8<\/span><\/em>, 5871\u20135877.\u00a0[pdf<\/a>] [doi]<\/a> [pubmed<\/a>]<\/p>\n

62. S. Mukherjee, S.P. Pondaven, K. Hand, J. Madine, C.P. Jaroniec, Effect of amino acid mutations on the conformational dynamics of amyloidogenic immunoglobulin light-chains: A combined NMR and in silico<\/em> study,\u00a0Sci. Rep.<\/em>\u00a02017<\/strong>, 7<\/i>, 10339. [pdf<\/a>] [doi]<\/a> [pubmed<\/a>]<\/p>\n

61. T. Theint, P.S. Nadaud, D. Aucoin, J.J. Helmus, S.P. Pondaven, K. Surewicz, W.K. Surewicz, C.P. Jaroniec, Species-dependent structural polymorphism of Y145Stop prion protein amyloid revealed by solid-state NMR spectroscopy,\u00a0Nat. Commun.<\/em>\u00a02017<\/strong>, 8<\/i>, 753. [pdf<\/a>] [doi]<\/a> [pubmed<\/a>]
\n\u2022 OSU Research News Article<\/a><\/p>\n

60. T. Theint, P.S. Nadaud, K. Surewicz, W.K. Surewicz, C.P. Jaroniec, 13<\/sup>C and 15<\/sup>N chemical shift assignments of mammalian Y145Stop prion protein amyloid fibrils,\u00a0Biomol. NMR Assign.<\/em>\u00a02017<\/strong>, 11<\/em>, 75-80. [pdf]<\/a> [doi]<\/a> [pubmed]<\/a><\/p>\n

59. L.A. Baldwin, J.W. Crowe, M.D Shannon, C.P. Jaroniec, P.L. McGrier, 2D covalent organic frameworks with alternating triangular and hexagonal pores, Chem. Mater. <\/i>2015<\/b>, 27<\/i>, 6169-6172. [pdf]<\/a> [doi]<\/a><\/p>\n

58. M. Gao, S. Paul, C.D. Schwieters, Z.Q. You, H. Shao, J.M. Herbert, J.R. Parquette, C.P. Jaroniec, A structural model for a self-assembled nanotube provides insight into its exciton dynamics, J. Phys. Chem. C<\/i> 2015<\/b>, 119<\/i>, 13948-13956. [pdf]<\/a> [doi]<\/a> [pubmed]<\/a><\/p>\n

57. C.P. Jaroniec, Structural studies of proteins by paramagnetic solid-state NMR spectroscopy, J. Magn. Reson.<\/i> 2015<\/b>, 253<\/em>, 50-59. [pdf]<\/a> [doi]<\/a> [pubmed]<\/a><\/p>\n

56. T.F. Cunningham, M.D. Shannon, M.R. Putterman, R.J. Arachchige, I. Sengupta, M. Gao, C.P. Jaroniec, S. Saxena, Cysteine specific Cu2+<\/sup> chelating tags used as paramagnetic probes in double electron electron resonance, J. Phys. Chem. B<\/i> 2015<\/b>, 119<\/i>, 2839-2843. [pdf]<\/a> [doi]<\/a> [pubmed]<\/a><\/p>\n

55. 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<\/i> 2015<\/b>, 61<\/i>, 1-6. [pdf]<\/a> [doi]<\/a>[pubmed]<\/a><\/p>\n

54. 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.<\/i> 2013<\/b>,135<\/i>, 19237-19247. [pdf]<\/a> [doi]<\/a> [pubmed]<\/a><\/p>\n

53. 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.<\/i> 2013<\/b>, 135<\/i>, 15278-15281. [pdf]<\/a> [doi]<\/a>[pubmed]<\/a><\/p>\n

52. I. Sengupta, P.S. Nadaud, C.P. Jaroniec, Protein structure determination with paramagnetic solid-state NMR spectroscopy, Acc. Chem. Res.<\/i> 2013<\/b>, 46<\/i>, 2117-2126. [pdf]<\/a> [doi]<\/a> [pubmed]<\/a><\/p>\n

51. J.J. Helmus, C.P. Jaroniec, Nmrglue: An open source Python package for the analysis of multidimensional NMR data, J. Biomol. NMR<\/i> 2013<\/b>, 55<\/i>, 355-367. [pdf]<\/a>\u00a0[doi]<\/a> [pubmed]<\/a><\/p>\n

50. 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-\u03b2 amyloid fibril, Proc. Natl. Acad. Sci. USA<\/i> 2013<\/b>,110<\/i>, 5468-5473. [pdf]<\/a> [doi]<\/a> [pubmed]<\/a>
\n\u2022 Physics Today Article<\/a><\/p>\n

49. 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 \u03b2-sheet and comparison with DEER spectroscopy, Biochemistry<\/i> 2012<\/b>, 51<\/i>, 6350-6359. [pdf]<\/a> [doi]<\/a> [pubmed]<\/a><\/p>\n

48. C.P. Jaroniec, Solid-state nuclear magnetic resonance structural studies of proteins using paramagnetic probes, Solid State Nucl. Magn. Reson.<\/i> 2012<\/b>, 43-44<\/i>, 1-13. [pdf]<\/a> [doi]<\/a>[pubmed]<\/a><\/p>\n

47. 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.<\/i> 2012<\/b>, 4<\/i>, 410-417. [pdf]<\/a> [doi]<\/a> [pubmed]<\/a>
\n\u2022 OSU Research News Article<\/a>
\n\u2022 spectroscopyNOW.com Article<\/a><\/p>\n

46. 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.<\/i> 2011<\/b>, 286<\/i>, 42777-42784. [pdf]<\/a> [doi]<\/a> [pubmed]<\/a><\/p>\n

45. 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.<\/i> 2011<\/b>, 17<\/i>, 12882-12885. [pdf]<\/a>[doi]<\/a> [pubmed]<\/a><\/p>\n

44. 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.<\/i> 2011<\/b>, 133<\/i>, 13934-13937. [pdf]<\/a> [doi]<\/a> [pubmed]<\/a><\/p>\n

43. 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 of15<\/sup>N longitudinal paramagnetic relaxation enhancements in proteins by solid-state NMR, J. Biomol. NMR<\/i> 2011<\/b>, 51<\/i>, 293-302. [pdf]<\/a> [doi]<\/a> [pubmed]<\/a><\/p>\n

42. 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<\/i> 2011<\/b>, 50<\/i>, 5845-5857. [pdf]<\/a> [doi]<\/a> [pubmed]<\/a><\/p>\n

41. 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.<\/i> 2010<\/b>, 132<\/i>, 9561-9563. [pdf]<\/a>\u00a0[doi]<\/a> [pubmed]<\/a><\/p>\n

40. 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.<\/i> 2010<\/b>, 49<\/i>, 7688-7691. [pdf]<\/a> [doi]<\/a> [pubmed]<\/a><\/p>\n

39. 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.<\/i> 2010<\/b>, 132<\/i>, 2393-2403. [pdf]<\/a> [doi]<\/a> [pubmed]<\/a><\/p>\n

38. 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<\/i>, J. Biol. Chem.<\/i>2010<\/b>, 285<\/i>, 2438-2455. [pdf]<\/a> [doi]<\/a> [pubmed]<\/a> *Cover article.
\n\u2022 JBC Paper of the Week<\/a><\/p>\n

37. P.S. Nadaud, M. Sarkar, B. Wu, C.E. MacPhee, T.J. Magliery, C.P. Jaroniec, Expression and purification of a recombinant amyloidogenic peptide from transthyretin for solid-state NMR spectroscopy, Protein Expr. Purif.<\/i> 2010<\/b>, 70<\/i>, 101-108. [pdf]<\/a>\u00a0[doi]<\/a> [pubmed]<\/a><\/p>\n

36. S. Mukherjee, S.P. Pondaven, N. H\u00f6fer, C.P. Jaroniec, Backbone and sidechain 1<\/sup>H, 13<\/sup>C and 15<\/sup>N resonance assignments of LEN, a human immunoglobulin \u03baIV light-chain variable domain, Biomol. NMR Assign.<\/i> 2009<\/b>, 3<\/i>, 255-259. [pdf]<\/a>\u00a0[doi]<\/a> [pubmed]<\/a><\/p>\n

35. C.P. Jaroniec, Dipolar Recoupling: Heteronuclear, In Encyclopedia of Magnetic Resonance<\/i>, R.K. Harris and R.E. Wasylishen, Eds., John Wiley, Chichester, 2009<\/b>. [pdf]<\/a>[doi]<\/a><\/p>\n

34. 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.<\/i> 2009<\/b>, 131<\/i>, 8108-8120. [pdf]<\/a> [doi]<\/a> [pubmed]<\/a><\/p>\n

33. V. Cherezov, N. H\u00f6fer, D.M.E. Szebenyi, O. Kolaj, J.G. Wall, R. Gillilan, V. Srinivasan, C.P. Jaroniec, M. Caffrey, Insights into the mode of action of a putative zinc transporter CzrB inThermus thermophilus<\/i>, Structure<\/i> 2008<\/b>, 16<\/i>, 1378-1388. [pdf]<\/a> [doi]<\/a> [pubmed]<\/a> *Cover article.<\/p>\n

32. 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<\/i> 2008<\/b>, 105<\/i>, 6284-6289. [pdf]<\/a>\u00a0[doi]<\/a> [pubmed]<\/a>
\n\u2022 OSU Research News Article<\/a><\/p>\n

31. J.J. Helmus, P.S. Nadaud, N. H\u00f6fer, C.P. Jaroniec, Determination of methyl 13<\/sup>C-15<\/sup>N dipolar couplings in peptides and proteins by three-dimensional and four-dimensional magic-angle spinning solid-state NMR spectroscopy, J. Chem. Phys.<\/i> 2008<\/b>, 128<\/i>, 052314.\u00a0[pdf]<\/a>\u00a0[doi<\/a>]\u00a0[pubmed]<\/a><\/p>\n

30. P.S. Nadaud, J.J. Helmus, C.P. Jaroniec, 13<\/sup>C and 15<\/sup>N chemical shift assignments and secondary structure of the B3 immunoglobulin-binding domain of streptococcal protein G by magic-angle spinning solid-state NMR spectroscopy, Biomol. NMR Assign.<\/i> 2007<\/b>, 1<\/i>, 117-120. [pdf]<\/a>\u00a0[doi]<\/a>\u00a0[pubmed]<\/a> *Cover article.<\/p>\n

29. P.S. Nadaud, J.J. Helmus, N. H\u00f6fer, C.P. Jaroniec, Long-range structural restraints in spin-labeled proteins probed by solid-state nuclear magnetic resonance spectroscopy, J. Am. Chem. Soc.<\/i> 2007<\/b>, 129<\/i>, 7502-7503. [pdf]<\/a>\u00a0[doi]<\/a> [pubmed]<\/a><\/p>\n

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28. C.P. Jaroniec, J.D. Kaufman, S.J. Stahl, M. Viard, R. Blumenthal, P.T. Wingfield, A. Bax, Structure and dynamics of micelle-associated human immunodeficiency virus gp41 fusion domain,Biochemistry<\/i> 2005<\/b>, 44<\/i>, 16167-16180. [pdf]<\/a>\u00a0[doi]<\/a> [pubmed]<\/a>
\n\u2022 Faculty of 1000 Biology Recommended<\/a><\/p>\n

27. C.P. Jaroniec, J. Boisbouvier, I. Tworowska, E. P. Nikonowicz, A. Bax, Accurate measurement of15<\/sup>N-13<\/sup>C residual dipolar couplings in nucleic acids, J. Biomol. NMR<\/i> 2005<\/b>, 31<\/i>, 231-241. [pdf]<\/a>\u00a0[doi]<\/a> [pubmed]<\/a><\/p>\n

26. C.P. Jaroniec, T.S. Ulmer, A. Bax, Quantitative J correlation methods for the accurate measurement of 13<\/sup>C\u2019-13<\/sup>C\u03b1 dipolar couplings in proteins, J. Biomol. NMR<\/i> 2004<\/b>, 30<\/i>, 181-194.[pdf]<\/a>\u00a0[doi]<\/a> [pubmed]<\/a><\/p>\n

25. C.P. Jaroniec, C.E. MacPhee, V.S. Bajaj, M.T. McMahon, C.M. Dobson, R.G. Griffin, High resolution molecular structure of a peptide in an amyloid fibril determined by magic angle spinning NMR spectroscopy, Proc. Natl. Acad. Sci. USA<\/i> 2004<\/b>, 101<\/i>, 711-716. [pdf]<\/a>\u00a0[doi]<\/a> [pubmed]<\/a>
\n\u2022 C&E News Science Concentrates Article<\/a>
\n\u2022 spectroscopyNOW.com Article<\/a><\/p>\n

24. V. Ladizhansky, C.P. Jaroniec, A. Diehl, H. Oschkinat, R.G. Griffin, Measurement of multiple \u03c8 torsion angles in U-13<\/sup>C,15<\/sup>N labeled a-spectrin SH3 domain using 3D 15<\/sup>N-13<\/sup>C-13<\/sup>C-15<\/sup>N MAS dipolar-chemical shift correlation spectroscopy, J. Am. Chem. Soc<\/i>. 2003<\/b>, 125<\/i>, 6827-6833. [pdf]<\/a>\u00a0[doi]<\/a>\u00a0[pubmed]<\/a><\/p>\n

23. C.P. Jaroniec, C.E. MacPhee, N.S. Astrof, C.M. Dobson, R.G. Griffin, Molecular conformation of a peptide fragment of transthyretin in an amyloid fibril, Proc. Natl. Acad. Sci. USA<\/i> 2002<\/b>, 99<\/i>, 16748-16753. [pdf]<\/a>\u00a0[doi]<\/a> [pubmed]<\/a>
\n\u2022 Faculty of 1000 Biology Must Read<\/a><\/p>\n

22. C.M. Rienstra, M. Hohwy, L.J. Mueller, C.P. Jaroniec, B. Reif, R.G. Griffin, Determination of multiple torsion-angle constraints in U-13<\/sup>C,15<\/sup>N-labeled peptides: 3D 1<\/sup>H-15<\/sup>N-13<\/sup>C-1<\/sup>H dipolar-chemical shift NMR spectroscopy in rotating solids, J. Am. Chem. Soc.<\/i> 2002<\/b>, 124<\/i>, 11908-11922.[pdf]<\/a>\u00a0[doi]<\/a> [pubmed]<\/a><\/p>\n

21. C.P. Jaroniec, C. Filip, R.G. Griffin, 3D TEDOR NMR experiments for the simultaneous measurement of multiple carbon-nitrogen distances in uniformly 13<\/sup>C,15<\/sup>N labeled solids, J. Am. Chem. Soc.<\/i> 2002<\/b>, 124<\/i>, 10728-10742. [pdf]<\/a>\u00a0[doi]<\/a> [pubmed]<\/a><\/p>\n

20. C.M. Rienstra, L. Tucker-Kellogg, C.P. Jaroniec, M. Hohwy, B. Reif, M.T. McMahon, B. Tidor, T. Lozano-Perez, R.G. Griffin, De novo<\/i> determination of peptide structure with solid-state magic-angle spinning NMR spectroscopy, Proc. Natl. Acad. Sci. USA<\/i> 2002<\/b>, 99<\/i>, 10260-10265. [pdf]<\/a>\u00a0[doi]<\/a>\u00a0[pubmed]<\/a><\/p>\n

19. A.T. Petkova, M. Hatanaka, C.P. Jaroniec, J.G. Hu, M. Belenky, M. Verhoeven, J. Lugtenburg, R.G. Griffin, J. Herzfeld, Tryptophan interactions in bacteriorhodopsin: A heteronuclear solid-state NMR study, Biochemistry<\/i> 2002<\/b>, 41<\/i>, 2429-2437. [pdf]<\/a>\u00a0[doi]<\/a> [pubmed]<\/a><\/p>\n

18. J.C. Lansing, M. Hohwy, C.P. Jaroniec, A.F.L. Creemers, J. Lugtenburg, J. Herzfeld, R.G. Griffin, Chromophore distortions in the bacteriorhodopsin photocycle: Evolution of the H-C14-C15-H dihedral angle measured by solid-state NMR, Biochemistry<\/i> 2002<\/b>, 41<\/i>, 431-438. [pdf]<\/a>\u00a0[doi]<\/a>\u00a0[pubmed]<\/a><\/p>\n

17. J.C. Lansing, M. Hohwy, C.P. Jaroniec, A. Creemers, J. Lugtenburg, J. Herzfeld, R.G. Griffin, Determination of torsion angles in membrane proteins, In Perspectives on Solid State NMR in Biology<\/i>, S. Kiihne, H.J.M. de Groot, Eds., Kluwer, Dordrecht, 2001<\/b>, 185-190.\u00a0[pdf]<\/a><\/p>\n

16. C.P. Jaroniec, B.A. Tounge, J. Herzfeld, R.G. Griffin, Accurate 13<\/sup>C\u201315<\/sup>N distance measurements in uniformly 13<\/sup>C,15<\/sup>N-labeled peptides, In Perspectives on Solid State NMR in Biology<\/i>, S. Kiihne, H.J.M. de Groot, Eds., Kluwer, Dordrecht, 2001<\/b>, 15-21.\u00a0[pdf]<\/a><\/p>\n

15. C.P. Jaroniec, J.C. Lansing, B.A. Tounge, M. Belenky, J. Herzfeld, R.G. Griffin, Measurement of dipolar couplings in a uniformly 13<\/sup>C,15<\/sup>N labeled membrane protein: Distances between the Schiff base and aspartic acids in the active site of bacteriorhodopsin, J. Am. Chem. Soc.<\/i> 2001<\/b>, 123<\/i>, 12929-12930. [pdf]<\/a>\u00a0[doi]<\/a> [pubmed]<\/a><\/p>\n

14. B. Reif, C.P. Jaroniec, C.M. Rienstra, M. Hohwy, R.G. Griffin, 1<\/sup>H-1<\/sup>H MAS correlation spectroscopy and distance measurements in a deuterated peptide, J. Magn. Reson.<\/i> 2001<\/b>, 151<\/i>, 320-327.[pdf]<\/a>\u00a0[doi]<\/a> [pubmed]<\/a><\/p>\n

13. C.P. Jaroniec, B.A. Tounge, J. Herzfeld, R.G. Griffin, Frequency selective heteronuclear dipolar recoupling in rotating solids: Accurate 13<\/sup>C\u201315<\/sup>N distance measurements in uniformly 13<\/sup>C,15<\/sup>N-labeled peptides, J. Am. Chem. Soc.<\/i> 2001<\/b>, 123<\/i>, 3507-3519. [pdf]<\/a>\u00a0[doi]<\/a> [pubmed]<\/a><\/p>\n

12. C.P. Jaroniec, B.A. Tounge, C.M. Rienstra, J. Herzfeld, R.G. Griffin, Recoupling of heteronuclear dipolar interactions with rotational-echo double-resonanace at high magic-angle spinning frequencies, J. Magn. Reson.<\/i> 2000<\/b>, 146<\/i>, 132-139. [pdf]<\/a>\u00a0[doi]<\/a> [pubmed]<\/a><\/p>\n

11. B. Reif, M. Hohwy, C.P. Jaroniec, C.M. Rienstra, R.G. Griffin, NH-NH vector correlation in peptides by solid-state NMR, J. Magn. Reson.<\/i> 2000<\/b>, 145<\/i>, 132-141. [pdf]<\/a>\u00a0[doi]<\/a> [pubmed]<\/a><\/p>\n

10. M. Hohwy, C.P. Jaroniec, B. Reif, C.M. Rienstra, R.G. Griffin, Local structure and relaxation in solid-state NMR: Accurate measurement of amide N-H bond lengths and H-N-H bond angles, J. Am. Chem. Soc.<\/i> 2000<\/b>, 122<\/i>, 3218-3219. [pdf]<\/a>\u00a0[doi]<\/a><\/p>\n

9. C.P. Jaroniec, B.A. Tounge, C.M. Rienstra, J. Herzfeld, R.G. Griffin, Measurement of 13<\/sup>C-15<\/sup>N distances in uniformly 13<\/sup>C labeled biomolecules: J-decoupled REDOR, J. Am. Chem. Soc.<\/i> 1999<\/b>,121<\/i>, 10237-10238. [pdf]<\/a>\u00a0[doi]<\/a><\/p>\n

8. M. Hohwy, C.M. Rienstra, C.P. Jaroniec, R.G. Griffin, Fivefold symmetric homonuclear dipolar recoupling in rotating solids: Application to double quantum spectroscopy, J. Chem. Phys.<\/i> 1999<\/b>,110<\/i>, 7983-7992. [pdf]<\/a>\u00a0[doi]<\/a><\/p>\n

7. M. Jaroniec, C.P. Jaroniec, M. Kruk, R. Ryoo, Adsorption and thermogravimetric methods for monitoring surface and structural changes in ordered mesoporous silicas induced by their chemical modification, Adsorption<\/i> 1999<\/b>, 5<\/i>, 313-317. [pdf]<\/a>\u00a0[doi]<\/a><\/p>\n

6. M. Jaroniec, M. Kruk, C.P. Jaroniec, A. Sayari, Modification of surface and structural properties of ordered mesoporous silicates, Adsorption<\/i> 1999<\/b>, 5<\/i>, 39-45. [pdf]<\/a>\u00a0[doi]<\/a><\/p>\n

5. C.P. Jaroniec, M. Kruk, M. Jaroniec, A. Sayari, Tailoring surface and structural properties of MCM\u201141 silicas by bonding organosilanes, J. Phys. Chem. B<\/i> 1998<\/b>, 102<\/i>, 5503-5510. [pdf]<\/a>\u00a0[doi]<\/a><\/p>\n

4. Y.D. Glinka, C.P. Jaroniec, M. Jaroniec, Studies of surface properties of disperse silica and alumina by luminescence measurements and nitrogen adsorption, J. Colloid Interface Sci.<\/i> 1998<\/b>,201<\/i>, 210-219. [pdf]<\/a>\u00a0[doi]<\/a><\/p>\n

3. C.P. Jaroniec, R.K. Gilpin, M. Jaroniec, Comparative studies of chromatographic properties of silica-based amide bonded phases under hydro-organic conditions, J. Chromatogr. A<\/i> 1998<\/b>, 797<\/i>, 103-110. [pdf]<\/a>\u00a0[doi]<\/a><\/p>\n

2. C.P. Jaroniec, M. Jaroniec, M. Kruk, Comparative studies of structural and surface properties of porous inorganic oxides used in liquid chromatography, J. Chromatogr.<\/i> A<\/i> 1998<\/b>, 797<\/i>, 93-102.[pdf]<\/a>\u00a0[doi]<\/a><\/p>\n

1. C.P. Jaroniec, R.K. Gilpin, M. Jaroniec, Adsorption and thermogravimetric studies of silica-based amide bonded phases, J. Phys. Chem. B<\/i> 1997<\/b>, 101<\/i>, 6861-6866. [pdf]<\/a>\u00a0[doi]<\/a><\/p>\n","protected":false},"excerpt":{"rendered":"

Google Scholar\u00a0\u00a0\u00a0\u00a0\u00a0 ResearcherID\u00a0\u00a0\u00a0\u00a0\u00a0 MyNCBI 85. B.P. Tatman, V. Sridharan, M. Uttarkabat, C.P. Jaroniec, M. Ernst, P. Rovo, P. Schanda, Bumps on the road: The way to clean relaxation dispersion magic-angle spinning NMR, J. Am. Chem. Soc. 2025, 147, 29315\u201329326. [pdf] [doi] [pubmed] 84. V. Sridharan, T. George, D.W. Conroy, Z. Shaffer, W.K. Surewicz, C.P. Jaroniec, […]<\/p>\n","protected":false},"author":4,"featured_media":0,"parent":0,"menu_order":0,"comment_status":"closed","ping_status":"closed","template":"","meta":{"footnotes":""},"class_list":["post-25","page","type-page","status-publish","hentry"],"_links":{"self":[{"href":"https:\/\/research.cbc.osu.edu\/jaroniec.1\/wp-json\/wp\/v2\/pages\/25","targetHints":{"allow":["GET"]}}],"collection":[{"href":"https:\/\/research.cbc.osu.edu\/jaroniec.1\/wp-json\/wp\/v2\/pages"}],"about":[{"href":"https:\/\/research.cbc.osu.edu\/jaroniec.1\/wp-json\/wp\/v2\/types\/page"}],"author":[{"embeddable":true,"href":"https:\/\/research.cbc.osu.edu\/jaroniec.1\/wp-json\/wp\/v2\/users\/4"}],"replies":[{"embeddable":true,"href":"https:\/\/research.cbc.osu.edu\/jaroniec.1\/wp-json\/wp\/v2\/comments?post=25"}],"version-history":[{"count":84,"href":"https:\/\/research.cbc.osu.edu\/jaroniec.1\/wp-json\/wp\/v2\/pages\/25\/revisions"}],"predecessor-version":[{"id":1015,"href":"https:\/\/research.cbc.osu.edu\/jaroniec.1\/wp-json\/wp\/v2\/pages\/25\/revisions\/1015"}],"wp:attachment":[{"href":"https:\/\/research.cbc.osu.edu\/jaroniec.1\/wp-json\/wp\/v2\/media?parent=25"}],"curies":[{"name":"wp","href":"https:\/\/api.w.org\/{rel}","templated":true}]}}