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
Dept. of Structural Biology
- Hoop CL, Lin HK, Kar K, Magyarfalvi G, Lamley JM, Boatz JC, Mandal A, Lewandowski JR, Wetzel R, van der Wel PC. Huntingtin exon 1 fibrils feature an interdigitated β-hairpin-based polyglutamine core. Proc Natl Acad Sci U S A. 2016;113(6):1546-51
- Merg AD, Boatz JC, Mandal A, Zhao G, Mokashi-Punekar S, Liu C, Wang X, Zhang P, van der Wel PC, Rosi NL. Peptide-Directed Assembly of Single-Helical Gold Nanoparticle Superstructures Exhibiting Intense Chiroptical Activity. J Am Chem Soc. 2016 in press
- Mandal A, Boatz JC, Wheeler T, Van der Wel PC On the use of ultracentrifugal devices for routine sample preparation in biomolecular magic-angle-spinning NMR J. Biomol. NMR 2017 in press