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Assistant Professor
75% Biological Sciences, 25% Chemistry
  • 765-494-4909
  • HOCK 231


Protein ultrastructures involved in virus-host interaction and other systems, development of cryo fluorescence microscopy applications.


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Large protein ultrastructures are prevalent in biology, with diverse functions ranging from heartbeats to viral infection.  While conformations and dynamics of protein monomers in solution have been well studied, their organization and coordinated functions within the complex chemical and physical environments of the cell are less well understood yet critical for the development of medical therapies and biotechnology.  My group uses an array of techniques, including cryo electron tomography, correlated light and electron microscopy, and fluorescence spectroscopy, to study protein ultrastructures involved in virus-host interaction and bacterial microcompartment function.

In addition to our biological areas of interest, we also develop new fluorescence-based approaches in correlated light and electron microscopy (cryo-CLEM).  We work to adapt room-temperature fluorescence-based tools to cryo electron tomography conditions in order to add additional information to the images.  A recent example of this was a fluorescence quenching-based fusion assay adapted to cryo temperatures, which enables a user to distinguish between visually-identical tomography images of membrane mixing and membrane apposition.

My group is currently accepting graduate students.

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