Master’s in Chemistry

Chemistry research in the Burdette group occurs at the interface of synthesis, metal ion homeostasis & signaling, cell biology and photochemistry. The group is developing molecular tools that will facilitate efforts to map cellular metal ion signaling pathways, and understand the pathologies of neurodegenerative diseases. Of particular interest is the development of photocaged complexes that are capable of releasing zinc in a light-dependent manner in biological systems. These tools are designed and synthesized to optimize the temporal and spatial control of zinc release.

Our research integrates investigating the structure and function of targeted membrane proteins with development of mixed reality tools for workforce development. We combine biochemical and biophysical techniques to investigate the structure and function of two classes of membrane proteins. In the first instance, we are investigating the mechanism of a zinc transporter, hZIP4. This protein has been implicated in the initiation and progression of pancreatic cancer. Despite the central role of this protein in cellular homeostasis, the mechanism of cation transport is not well understood.

What makes a particular material efficient at converting sunlight to electrical or chemical energy? Conversely, what makes a material a poor energy converter? The Grimmgroup is motivated by quantifying and controlling the bulk and surface properties of solar energy conversion materials. As a research group in the Department of Chemistry and Biochemistry at Worcester Polytechnic Institute, we seek an atom- and bond-level understanding of material properties.

I am a computational physical chemist. My research is in the areas of force field building and applications. Special attention is given to creating polarizable force fields for organic and biophysical systems, including proteins and protein-ligand complexes. I teach classes in physical, computational and general chemistry. Simulations of proteins is very important in biomedical research because proteins play crucial role in a large number of biological phenomena, both benign and harmful.

Research in the Mattson Group is a combination of catalyst design, methodology development, and complex molecule synthesis. Our catalyst design program is focused on the synthesis and study of new families of non-covalent catalysts, including boronate ureas and silanediols, that are able to promote new reactivity patterns. The catalyst design and associated reaction development programs are currently geared toward the synthesis of enantioenriched nitrogen and oxygen heterocycles that frequently appear in naturally occurring bioactive compounds.

Membranes are composed of hundreds of distinct kinds of phospholipids, and the types of lipids that are found within a membrane bilayer impact its biophysical properties including its fluidity, permeability and susceptibility to damage. Our primary interest is in understanding the mechanisms that control the phospholipid composition and that preserve the membrane over time. We use stable isotope tracing strategies and mass spectrometry to quantify phospholipid abundance and dynamics in the model organism, C. elegans.

Suzanne Scarlata, Richard Whitcomb Professor of Chemistry and Biochemistry, joined the university faculty in 2016. She studies how small molecules in the bloodstream can change the behavior of cells. In particular, she is interested in how certain hormones and neurotransmitters can activate a family of organic molecules known as G proteins (guanine nucleotide-binding proteins), which are involved in transmitting signals from various stimuli from the exterior to the interior of cells.