ACS

November 2017 Meeting - Akron Section Award

(posted on Thursday, October 26, 2017)

The Akron Section of the American Chemical Society has conferred its Akron Section Award on Christopher Jaroniec, Evans Professor of Chemistry at The Ohio State University and Director of Ohio State’s Solid-State NMR Center. Dr. Jaroniec will deliver an afternoon lecture at The University of Akron and give another talk during the evening program at Hiram College on November 14, 2017. The award will be presented during the evening program.  

The University of Akron-111 Mary Gladwin Hall

3:30 pm – Afternoon Lecture

Solid-State NMR Structural Studies of Proteins Using Paramagnetic Probes

Hiram College, Kennedy Center

5:30 pm – Networking and Poster Session

6:30 pm – Dinner ($25 for Professionals and Guests, $10 for Students)

7:15 pm – Evening Program

            Molecular Mechanisms of Prion and Amyloid Propagation Explored by Solid-State NMR Spectroscopy

The afternoon lecture and evening program are free and open to the public. Dinner reservations by Noon, Friday, November 10 to Walter Salamant.

Biography – Christopher Jaroniec

Christopher Jaroniec received his B.S. degree 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 with Prof. Robert Griffin, and he was a Damon Runyon Cancer Research Foundation Postdoctoral Fellow with Dr. Ad Bax at the National Institutes of Health. He joined The Ohio State University as an Assistant Professor in 2006, and was promoted to Associate Professor in 2011 and Professor in 2014. He currently holds the Evans Endowed Scholarship and serves as the Vice Chair for Research and Administration in the Department of Chemistry and Biochemistry at OSU, and is also the Director of the OSU CCIC Solid-State NMR Center, which houses multiple state-of-the-art high-field solid-state NMR instruments. Professor Jaroniec’s research interests are in the development and applications of advanced solid-state NMR methods for the determination of structure, dynamics and interactions of supramolecular protein and protein-DNA assemblies, including amyloids, prions and chromatin. His research has been recognized by multiple awards including the NSF CAREER Award, the Eli Lilly Young Investigator Award in Analytical Chemistry, the Camille Dreyfus Teacher-Scholar Award, the Founders' Medal from the International Council on Magnetic Resonance in Biological Systems, the Varian Young Investigator Award in Magnetic Resonance, and the ACS Physical Division Early-Career Award in Experimental Physical Chemistry. He was also elected as Fellow of the American Association for the Advancement of Science and has held an Invited Visiting Professor position at Sorbonne Universités/Université Pierre et Marie Curie in Paris, France.

Abstract – Afternoon Lecture

Solid-State NMR Structural Studies of Proteins Using Paramagnetic Probes

Structural studies of proteins by magic-angle spinning solid-state nuclear magnetic resonance (NMR) spectroscopy are generally hampered by the relative shortage of distance restraints exceeding ~5-6 Å, that can be reliably determined from measurements of magnetic dipole-dipole couplings between nuclear spins. This problem can be alleviated by using structural analogs of the protein of interest, intentionally modified to contain covalently-linked paramagnetic tags at specific sites. In such paramagnetic proteins, the dipolar couplings between the nuclear spins and the unpaired electrons of the tag manifest themselves in NMR spectra in the form of nuclear dipolar shifts or relaxation enhancements that depend on the electron-nucleus distance and can be considerable for nuclei located up to ~20 Å away from the paramagnetic center. I will discuss our recent advances in the development of multidimensional solid-state NMR techniques based on paramagnetic tagging. The topics discussed will include the de novo determination of the three-dimensional structure of a model globular protein based largely on paramagnetic restraints, development of resolution and sensitivity enhanced approaches and new metal-binding tags for the structural analysis of proteins by paramagnetic solid-state NMR, and applications of paramagnetic solid-state NMR methods to supramolecular amyloid protein assemblies.

Abstract – Evening Program

Molecular Mechanisms of Prion and Amyloid Propagation Explored by Solid-State NMR Spectroscopy

In this talk, the basics of structural and dynamic studies of biological macromolecules by magic-angle spinning solid-state nuclear magnetic resonance (NMR) spectroscopy will be introduced. The application of this methodology toward providing an atomic level understanding of the phenomena of amyloid strains and cross-seeding barriers in a family of mammalian prion protein variants will be discussed.






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