My group is primarily focused on understanding how the structure, dynamics, and/or stability of proteins change in diseased states. Students I’ve worked with have been involved in a number of fun and productive interdisciplinary collaborations that have allowed us to use the most relevant techniques to address questions we’re interested in. Some examples of proteins we have focused on in the past include the amyloid precursor protein (Alzheimer’s Disease) and its interaction with the kinesin light chain (a joint computation/wet lab project in collaboration with Carol Parish at University of Richmond), presenilins1 and 2 (early onset Alzheimer’s Disease), and ionotropic glutamate receptors (depression and neurodegenerative diseases). I’m also really interested in metabolon formation and substrate channeling in proteins. We’re currently working to engineer spectroscopic probes into malate dehydrogenase (MDH) so we can study substrate channeling between citric acid and malate dehydrogenase in the citric acid cycle. This is a project that is in collaboration with a group across the country working on different aspects of MDH. In all of these projects, we clone wild type and mutant proteins, over-express in E.coli, purify, and then ask questions about structure, dynamics, and/or stability using the most relevant technique for a particular protein.
I also enjoy working with students interested in asking questions about local issues. For example, I am currently working with a student to design a PCR-based eDNA screen to identify and differentiate between the invasive aquatic plant species Eurasian watermilfoil and Hydrilla verticillata in Raystown Lake (PA). This is a project that is in collaboration with Sharon Yohn, a water chemist at Juniata College.