Chemistry Faculty Research

Analytical Chemistry Research

Professor Kim Frederick's research group develops miniaturized devices for conducting biomedical and environmental analysis.  Our devices employ microfluidic or “lab on a chip” technology to make devices that are smaller, less expensive and faster.  Current projects include developing a lab on a CD player in order to do urine-based testing for malaria, a disease which kills millions every year.  We are also developing automated water quality monitoring platforms to test underground and surface water for organic contaminants.

Biochemistry Research

Professor Kelly Sheppard's research group is interested in the different pathways organisms use to translate the genetic code, in particular with regard to the amino acid asparagine (Asn). The work provides insight not only into the life cycles of these bacteria but also into the evolution of the Asn decoding pathways. The research also lays the foundation for development of new antibiotics to target these pathogenic bacteria. We are also applying our knowledge of these pathways to expand the genetic code to incorporate unnatural amino acids into proteins to facilitate studies on Alzheimer’s Disease and more active anti-cancer agents.

Professor Raththagala’s research group studies the structure-function relationship of proteins involved in reversible starch phosphorylation. Our specific interest is to define the molecular mechanism of starch dephosphorylation by the glucan phosphatase Starch Excess4. We employ a variety of biochemical and biophysical techniques including x-ray crystallography, small angle x-ray scattering, differential scanning fluorimetry and enzymatic assays to decipher the molecular basis of glucan phosphatases. The information we obtain will enable us to develop a cost-effective, environmental friendly strategy to harness starch in an industrial setting.

Bioinorganic and Inorganic Chemistry Research

Professor Steven Frey's research group has two main interests.  The first is to produce composites by immobilizing metal ions, metal complexes, or biological molecules on solid-state materials. Applications of these composite materials include catalysis, optical information storage, and the detoxification of environmental pollutants.  The second is in the synthesis of transition metal complexes as models for the active site centers of metalloenzymes.

Computational Biophysics

Professor Lia Ball's research program uses computer simulations and other computational methods to study how intrinsically disordered proteins (IDPs) interact with folded proteins in the context of disease, or as part of normal cellular function. IDPs are different from typical folded proteins in that they lack a single well-defined structure and instead dynamically occupy many alternate structures. This research draws on knowledge from physics, chemistry, biology, and computer science to understand the fundamental physical principles governing interactions between disordered and folded proteins and how these interactions are important for their function. 

Organic Chemistry Research

Professor Jessada Mahatthananchai's undergraduate research group in synthetic chemistry focuses on developing new methodologies that are versatile and simple to operate to label organic molecules with deuterium, taking inspiration from nature’s catalysts. Students in our laboratory will learn advanced theories of the underlying reaction mechanisms, as well as techniques for preparing and characterizing new molecular entities with modern instrumentation such as NMR, IR, and GC/MS. 

Physical Chemistry Research

Professor Juan Navea’s research group combines experimental and theoretical methods to study the impact of atmospheric aerosols in the physics and chemistry of the troposphere (lower atmosphere). Daytime and nighttime chemistry is simulated using particles from dust storms, volcanos, and/or human activities.

Quantum Computational Chemistry Research

Professor William Kennerly's research group investigates the fluorescence of tryptophan, an essential amino acid.  Biochemists use the light emitted from an individual tryptophan residue in a large protein molecule to figure out how the protein molecule moves, which is essential towards understanding its function in vivo.  Quantum chemistry methods are the best way to answer detailed questions about the protein:  what wavelength of light will it absorb and emit?  How does that change if the protein is folded, or not, or exposed to solvent, or not?  Students working with Prof. Kennerly learn how to apply quantum mechanical ideas to understand chemical properties using research-grade software and high-performance computers.