Kent Thurber, Ph.D.

Research Goal

The goal is to determine and characterize protein structures that are important for human biology, such as amyloid fibrils, protein folding intermediates, or hormone/receptor complexes.

Current Research

My research is focused on protein structure determination using solid-state nuclear magnetic resonance (NMR) and electron microscopy (EM). Current projects include optimizing cryogenic-EM of amyloid fibrils, and using dynamic nuclear polarization (DNP) for solid-state NMR experiments on biomolecules. DNP can increase the NMR signal by 100 times or more, enabling experiments on small samples, or dilute samples, that would not be feasible otherwise. We have developed a custom NMR probe for DNP and magic-angle spinning (MAS) at low temperatures (25 K).

Applying our Research

The purpose of the research is to determine protein structures that are relevant for human diseases, for example the Abeta amyloid fibrils found in Alzheimer’s disease. The development of dynamic nuclear polarization for solid-state NMR may also have benefits to other areas, such as materials research.

Need for Further Study

Now that dynamic nuclear polarization (DNP) for solid-state nuclear magnetic resonance (NMR) has been developed, many biomolecules could potentially be studied. In addition, the optimum measurement conditions for biomolecular solid-state NMR with DNP are not well understood.

Research in Plain Language

My research improves the accuracy of tools we use to study the 3-dimensional structure of proteins. One important part of my work involves a process that will make it possible to study very small or dilute samples.