About

Christopher Jaroniec is Arts and Sciences Distinguished Professor and Associate Dean for Research and Creative Inquiry in the College of Arts and Sciences at The Ohio State University. He received his B.S. in Chemistry from Kent State University in 1997 and his Ph.D. in Physical Chemistry from the Massachusetts Institute of Technology in 2003, where he was a National Science Foundation Graduate Research Fellow. He also completed postdoctoral research as a Damon Runyon Cancer Research Foundation Fellow at the National Institutes of Health. Jaroniec joined Ohio State as an Assistant Professor in 2006, was promoted to Associate Professor in 2011, and to Professor in 2014. He was named Evans Scholar in 2013 and College of Arts and Sciences Distinguished Professor in 2021. Currently, he also serves as Associate Director of the OSU CCIC NMR Facility, directing operations of high-field solid-state NMR instruments. His research focuses on developing multidimensional magic-angle spinning solid-state NMR techniques and applying them to analyze molecular structure, conformational dynamics, and intermolecular interactions of biological macromolecules relevant to human health. His work employs complementary biophysical, computational, biochemical, and molecular biology methods, including solution-state NMR and cryo-electron microscopy. Jaroniec has received numerous national and international awards, including the NSF CAREER Award, Eli Lilly Young Investigator Award, Camille Dreyfus Teacher-Scholar Award, and he is a Fellow of the AAAS.

Research topics

• Chemistry
• Crystallography
• Nuclear magnetic resonance
• Biophysics
• Materials science

Selected publications

• Bumps on the Road: The Way to Clean Relaxation Dispersion Magic-Angle Spinning NMR

  Journal of the American Chemical Society · 2025-08-01 · 2 citations

  articleOpen access

  Microsecond-to-millisecond motions are instrumental for many biomolecular functions, including enzymatic activity and ligand binding. Bloch-McConnell Relaxation Dispersion (BMRD) Nuclear Magnetic Resonance (NMR) spectroscopy is a key technique for studying these dynamic processes. While BMRD experiments are routinely used to probe protein motions in solution, the experiment is more demanding in the solid state, where dipolar couplings complicate the spin dynamics. It is believed that high deuteration levels are required and sufficient to obtain accurate and quantitative data. Here we show that even under fast magic-angle spinning and high levels of deuteration artifactual “bumps” in 15N R1ρ BMRD profiles are common. The origin of these artifacts is identified as a second-order three-spin Mixed Rotational and Rotary Resonance (MIRROR) recoupling condition. These artifacts are found to be a significant confounding factor for the accurate quantification of microsecond protein dynamics using BMRD in the solid state. We show that the application of low-power continuous wave (CW) decoupling simultaneously with the 15N spin-lock leads to the suppression of these conditions and enables quantitative measurements of microsecond exchange in the solid state. Remarkably, the application of decoupling allows the measurement of accurate BMRD even in fully protonated proteins at 100 kHz MAS, thus extending the scope of μs dynamics measurements in MAS NMR.

  PublisherDOI

• Dnp Enhanced Solid-State Nmr of Protein Assemblies Facilitated by Co-Assembly with Dinitroxide-Tagged Proteins

  SSRN Electronic Journal · 2025-01-01

  preprintOpen accessSenior author
  PublisherDOI

• DNP enhanced solid-state NMR of lattice-like microcrystalline protein assemblies facilitated by co-assembly with dinitroxide-tagged proteins

  Journal of Magnetic Resonance · 2025-12-24

  articleOpen accessSenior authorCorresponding
  PublisherOA PDFDOI

• Impact of shared facilities in advancing solid-state NMR research: 2025 edition

  Solid State Nuclear Magnetic Resonance · 2025-11-28

  articleOpen access

  Shared research facilities (SRFs) offer researchers cost-effective access to advanced analytical instrumentation that individual laboratories may find challenging to acquire or maintain. By centralizing resources, SRFs support a diverse user community including students, early-career scientists, senior principal investigators, and industrial collaborators, while providing expert technical support and ensuring efficient use of infrastructure and funding. These facilities not only drive research productivity and foster interdisciplinary collaboration, but also serve as centers for training the next generation of scientists. In this article, SRFs that offer solid-state nuclear magnetic resonance (NMR) capabilities are discussed, highlighting representative examples, their accessibility, governance models, technical operations, application areas, and data-sharing practices. Usage data reveal that solid-state NMR-based SRFs strongly align with high-priority research goals, contributing to impactful projects across chemistry, life sciences, and materials science, as reflected in publication outcomes. The article also emphasizes that the collaborative networks among SRFs enhance knowledge exchange and resource coordination. Such coordinated inter-facility partnerships are expected to address emerging challenges, ultimately supporting sustainable infrastructure that meets the evolving needs of the solid-state NMR community.

  PublisherDOI

• Copper binding alters the core structure of amyloid fibrils formed by Y145Stop human prion protein

  Physical Chemistry Chemical Physics · 2024-01-01 · 6 citations

  articleOpen accessSenior authorCorresponding

  Binding of copper( ii ) to Y145Stop human prion protein leads to formation of an amyloid structural strain that is distinct from that obtained for amyloid fibrils of the same protein formed in the absence of bound copper( ii ).

  PublisherOA PDFDOI

• Insights into Ligand-Mediated Activation of an Oligomeric Ring-Shaped Gene-Regulatory Protein from Solution- and Solid-State NMR

  Journal of Molecular Biology · 2024-09-12 · 4 citations

  articleOpen access
  PublisherOA PDFDOI

• Structural and dynamic studies of chromatin by solid-state NMR spectroscopy

  Current Opinion in Structural Biology · 2024-09-17 · 6 citations

  reviewOpen access1st authorCorresponding
  PublisherOA PDFDOI

• Insights into Ligand-Mediated Activation of an Oligomeric Ring-Shaped Gene-Regulatory Protein from Solution- and Solid-State NMR

  bioRxiv (Cold Spring Harbor Laboratory) · 2024-05-14

  preprintOpen access

  Abstract The 91 kDa oligomeric ring-shaped ligand binding protein TRAP ( trp RNA binding attenuation protein) regulates the expression of a series of genes involved in tryptophan (Trp) biosynthesis in bacilli. When cellular Trp levels rise, the free amino acid binds to sites buried in the interfaces between each of the 11 (or 12, depending on the species) protomers in the ring. Crystal structures of Trp-bound TRAP show the Trp ligands are sequestered from solvent by a pair of loops from adjacent protomers that bury the bound ligand via polar contacts to several threonine residues. Binding of the Trp ligands occurs cooperatively, such that successive binding events occur with higher apparent affinity but the structural basis for this cooperativity is poorly understood. We used solution methyl-TROSY NMR relaxation experiments focused on threonine and isoleucine sidechains, as well as magic angle spinning solid-state NMR 13 C- 13 C and 15 N- 13 C chemical shift correlation spectra on uniformly labeled samples recorded at 800 and 1200 MHz, to characterize the structure and dynamics of the protein. Methyl 13 C relaxation dispersion experiments on ligand-free apo TRAP revealed concerted exchange dynamics on the µs-ms time scale, consistent with transient sampling of conformations that could allow ligand binding. Cross-correlated relaxation experiments revealed widespread disorder on fast timescales. Chemical shifts for methyl-bearing side chains in apo- and Trp-bound TRAP revealed subtle changes in the distribution of sampled sidechain rotameric states. These observations reveal a pathway and mechanism for induced conformational changes to generate homotropic Trp-Trp binding cooperativity.

  PublisherOA PDFDOI

• Conformational and Interaction Landscape of Histone H4 Tails in Nucleosomes Probed by Paramagnetic NMR Spectroscopy

  Journal of the American Chemical Society · 2023-11-09 · 18 citations

  articleOpen accessSenior authorCorresponding

  The fundamental repeat unit of chromatin, the nucleosome, consists of approximately 147 base pairs of double-stranded DNA and a histone protein octamer containing two copies each of histones H2A, H2B, H3, and H4. Each histone possesses a dynamically disordered N-terminal tail domain, and it is well-established that the tails of histones H3 and H4 play key roles in chromatin compaction and regulation. Here we investigate the conformational ensemble and interactions of the H4 tail in nucleosomes by means of solution NMR measurements of paramagnetic relaxation enhancements (PREs) in recombinant samples reconstituted with 15N-enriched H4 and nitroxide spin-label tagged H3. The experimental PREs, which report on the proximities of individual H4 tail residues to the different H3 spin-label sites, are interpreted by using microsecond time-scale molecular dynamics simulations of the nucleosome core particle. Collectively, these data enable improved localization of histone H4 tails in nucleosomes and support the notion that H4 tails engage in a fuzzy complex interaction with nucleosomal DNA.

  PublisherOA PDFDOI

• Mass-per-Length Measurements Using STEM in SEM

  Microscopy and Microanalysis · 2023-07-22

  articleOpen accessSenior author

  Journal Article Mass-per-Length Measurements Using STEM in SEM Get access Daniel P Veghte, Daniel P Veghte The Ohio State University, Center for Electron Microscopy and Analysis, Columbus, OH, USA Corresponding author: veghte.2@osu.edu Search for other works by this author on: Oxford Academic Google Scholar Christian M O’Neil, Christian M O’Neil The Ohio State University, Department of Chemistry and Biochemistry, Columbus, OH, USA Search for other works by this author on: Oxford Academic Google Scholar Sean Smrt, Sean Smrt The Ohio State University, Department of Chemistry and Biochemistry, Columbus, OH, USA Search for other works by this author on: Oxford Academic Google Scholar Giovanna Grandinetti, Giovanna Grandinetti The Ohio State University, Center for Electron Microscopy and Analysis, Columbus, OH, USA Search for other works by this author on: Oxford Academic Google Scholar Christopher Jaroniec Christopher Jaroniec The Ohio State University, Department of Chemistry and Biochemistry, Columbus, OH, USA Search for other works by this author on: Oxford Academic Google Scholar Microscopy and Microanalysis, Volume 29, Issue Supplement_1, 1 August 2023, Pages 1010–1011, https://doi.org/10.1093/micmic/ozad067.508 Published: 22 July 2023

  PublisherOA PDFDOI

Recent grants

• Molecular Mechanisms of Prion and Amyloid Propagation

  NIH · $3.2M · 2011–2024

• Structural Studies of Proteins by Paramagnetic Solid-State NMR Spectroscopy

  NSF · $932k · 2023–2027

• NIH Grant S10OD012303

  NIH · $2.0M · 2016

• CAREER: High-resolution Structural Studies of Paramagnetic Proteins by Multidimensional Solid-state NMR Spectroscopy

  NSF · $698k · 2008–2014

• NIH Grant R01GM123743

  NIH · $658k · 2021

Frequent coauthors

• Robert G. Griffin

  Massachusetts Institute of Technology

  53 shared

• Glenn L. Millhauser

  University of California, Santa Cruz

  36 shared

• Alexander Angerhofer

  University of Florida

  36 shared

• Christoph Boehme

  University of Utah

  36 shared

• Gary J. Gerfen

  Albert Einstein College of Medicine

  36 shared

• Guido Pintacuda

  École Normale Supérieure de Lyon

  36 shared

• Martin L. Kirk

  The Ohio State University

  36 shared

• Michael Bowman

  Iowa State University

  36 shared

Awards & honors

• CAREER Award from the National Science Foundation
• Eli Lilly Young Investigator Award in Analytical Chemistry
• Camille Dreyfus Teacher-Scholar Award
• Founders' Medal from the International Council on Magnetic R…
• Varian Young Investigator Award in Magnetic Resonance