U.S. Department of Health and Human Services
Kent Thurber

 Contact Info

Tel: 301-402-4687
Email: thurberk@mail.nih.gov

 Select Experience

  • Staff ScientistLaboratory of Chemical Physics, NIDDK, NIH2005-present
  • Postdoctoral FellowMaterials Magnetic Resonance Group, U.S. Naval Research Laboratory2003-2005
  • Postdoctoral FellowMagnetic Resonance Force Microscopy Group, U.S. Army Research Laboratory1999-2003
  • Ph.D.Massachusetts Institute of Technology1999
  • B.S.Massachusetts Institute of Technology1994

 Related Links

  • Biomedical Engineering/Biophysics/Physics
  • Nuclear Magnetic Resonance
Research Summary/In Plain Language

Research Summary

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).  My current primary project is developing 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.