
Christopher Jaroniec
Ohio State University · Biochemistry
Active 1997–2025
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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…
Research topics
- Chemistry
- Crystallography
- Nuclear magnetic resonance
- Biophysics
- Materials science
Selected publications
Sensitivity boosts by the CPMAS CryoProbe for challenging biological assemblies
Journal of Magnetic Resonance · 2019-12-23 · 81 citations
articleOpen accessHistone H4 Tails in Nucleosomes: a Fuzzy Interaction with DNA
Angewandte Chemie International Edition · 2021-02-01 · 40 citations
articleOpen accessSenior authorCorrespondingAbstract The interaction of positively charged N‐terminal histone tails with nucleosomal DNA plays an important role in chromatin assembly and regulation, modulating their susceptibility to post‐translational modifications and recognition by chromatin‐binding proteins. Here, we report residue‐specific 15 N NMR relaxation rates for histone H4 tails in reconstituted nucleosomes. These data indicate that H4 tails are strongly dynamically disordered, albeit with reduced conformational flexibility co…
Proceedings of the National Academy of Sciences · 2022-07-20 · 33 citations
articleOpen accessSenior authorThe majority of base pairs in double-stranded DNA exist in the canonical Watson-Crick geometry. However, they can also adopt alternate Hoogsteen conformations in various complexes of DNA with proteins and small molecules, which are key for biological function and mechanism. While detection of Hoogsteen base pairs in large DNA complexes and assemblies poses considerable challenges for traditional structural biology techniques, we show here that multidimensional dynamic nuclear polarization-enhanc…
Two decades of progress in structural and dynamic studies of amyloids by solid-state NMR
Journal of Magnetic Resonance · 2019-07-09 · 31 citations
reviewOpen access1st authorCorrespondingConformational Dynamics of Histone H3 Tails in Chromatin
The Journal of Physical Chemistry Letters · 2021-06-29 · 25 citations
articleOpen accessSenior authorCorrespondingChromatin is a supramolecular DNA–protein complex that compacts eukaryotic genomes and regulates their accessibility and functions. Dynamically disordered histone H3 N-terminal tails are among key chromatin regulatory components. Here, we used high-resolution-magic-angle-spinning NMR measurements of backbone amide 15N spin relaxation rates to investigate, with residue-specific detail, the dynamics and interactions of H3 tails in recombinant 13C,15N-enriched nucleosome arrays containing 15, 30, o…
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 · $2.0M · 2016
Frequent coauthors
- 53 shared
Robert G. Griffin
Massachusetts Institute of Technology
- 36 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
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
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