Research Interests:

I utilize a number of biophysical techniques to investigate the aggregation behavior of human gamma D crystallin (HGD) and investigate the protein’s structure in the aggregated state.  HGD is an extremely soluble and stable protein responsible for making the eye lens highly refractive.  When mutated or damaged, HGD can aggregate and participate in cataract formation.  In my experiments I make use of a variety of fluorescence-based assays, negative stain electron microscopy and X-ray powder diffraction. Moreover, I use multidimensional magic-angle-spinning (MAS) NMR to investigate the atomic structural details of aggregated HGD.  Comparison between solid and solution state NMR spectra allow for a site specific understanding of the structural changes HGD experiences upon aggregation.



Biology BS, Indiana University at Bloomington, 2013
Neuroscience BS, Indiana University at Bloomington, 2013

PhD Advisor: Angela Gronenborn & Patrick van der Wel

Lab Address: 

Dept. of Structural Biology

BST3 2054


email: jcb122{at}