Kent Thurber, Ph.D.
- Staff Scientist, Laboratory of Chemical Physics, NIDDK, NIH, 2005-present
- Postdoctoral Fellow, Materials Magnetic Resonance Group, U.S. Naval Research Laboratory, 2003-2005
- Postdoctoral Fellow, Magnetic Resonance Force Microscopy Group, U.S. Army Research Laboratory, 1999-2003
- Ph.D., Massachusetts Institute of Technology, 1999
- B.S., Massachusetts Institute of Technology, 1994
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.
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.
- Automated picking of amyloid fibrils from cryo-EM images for helical reconstruction with RELION.
- Thurber KR, Yin Y, Tycko R.
- J Struct Biol (2021 Jun) 213:107736. Abstract/Full Text
- Molecular structure of a prevalent amyloid-β fibril polymorph from Alzheimer's disease brain tissue.
- Ghosh U, Thurber KR, Yau WM, Tycko R.
- Proc Natl Acad Sci U S A (2021 Jan 26) 118. Abstract/Full Text
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.