Prof. Christopher Jaroniec, The Ohio State University

Solid-state NMR spectroscopy of protein assemblies

School Colloquium

Solid-state nuclear magnetic resonance has recently emerged as a unique spectroscopic tool, with great potential for generating atomic-resolution images of macromolecular assemblies that do not readily lend themselves to analysis by traditional high-resolution approaches. I will introduce the key aspects of magic-angle spinning solid-state NMR spectroscopy and describe the results of our recent studies aimed at providing molecular level insights into the mechanisms of fundamental biological phenomena that involve large protein-protein or protein-nucleic acid complexes, including prion and amyloid strains and transmissibility barriers linked to protein misfolding diseases as well as DNA compaction in chromatin. I will also highlight applications of this NMR methodology to the structural analysis of self-assembled organic nanomaterials formed from small molecule precursors, and discuss the development of a new class of magic-angle spinning NMR techniques for the rapid determination of protein structures in the solid phase based on the use of covalently-attached paramagnetic tags.

For more information contact Prof. Andrew Lyon (404-894-4090).