Christopher Jaroniec

Mentor Faculty
Professor
Department of Chemistry & Biochemistry

 

Research Description:


Research Interests:

Our research is centered on the development of multi-dimensional NMR techniques with the goal of providing insight into the structure and dynamics of biological macromolecules at atomic resolution. The primary focus of the group is on magic-angle spinning solid-state NMR. However, we are also interested in the development and application of modern NMR methods that provide site-specific structural information for partially-aligned molecules in solution and at the solid-liquid interface. The main applications will be to systems of profound importance in biology and medicine including supramolecular protein aggregates (often referred to as amyloid fibrils and discussed in more detail below), membrane-associated peptides and proteins, and large macromolecular complexes.

Amyloid fibrils are highly organized filamentous nanostructures formed by the self-assembly of peptide and protein molecules that in their soluble forms have a variety of secondary structures and functions. Some 20 proteins self-assemble into fibrils in vivo and are associated with very serious protein misfolding disorders including Alzheimer's disease, type II diabetes and the prion diseases. Despite significant interest and recent progress in the field much remains to be learned about the atomic structure of fibrils formed from different precursor molecules and the mechanism of fibril formation. We will use solid-state NMR to investigate the secondary structure and higher-order architecture of amyloid fibrils formed by several disease-related proteins, including the peptide hormone amylin associated with type II diabetes and a mammalian prion protein. Concurrently, conformational properties of amyloid intermediate states will be probed using solution-state NMR to provide further insight into the atomic-level events leading to the self-assembly of proteins into amyloid fibrils.

The research carried out in the group is highly interdisciplinary. In addition to multi-dimensional solution- and solid-state NMR, the lab will use computational and biophysical methods, and chemical and molecular biology approaches to synthesis and purification of isotope labeled peptides and proteins.

Education
  • Ph.D., Physical Chemistry, Massachusetts Institute of Technology, 2003
Students

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