Department of Chemistry

Faculty Research

The following is a synopsis of current research projects available to students.

Angela Peters (Prof. & Vice Provost of Academic Programs).

Research area is focused on the structural and functional analysis of mutant enzymes (Thymidylate Synthase). Studies include kinetic analysis, drug inhibition (resistance), antibody analysis, purification and growth complementation. Enzyme characterization utilizes UV-Vis, HPLC, FPLC and FTIR.

Governors Professor of the Year, 2005; National HBCU-UP Millennium Teaching Award, 2004; James Hunter Award for Teaching, 2004.

Muthukrishna Raja (Prof. /Organic Chemistry).

Research involves studying the potential “neighboring group effect” or “neighboring group mechanism” in catalytic carbonylation reactions of alkyl halides containing hetro atoms in the b-positions. One potential application of this study is the possibility of converting chemical warfare agents like mustard gas, S(CH2-CH2-Cl)2, to less toxic and potentially useful derivatives such as S(CH2-CH2-COOH)2 and/or S(CH2-CH2-COOR)2. Undergraduate researchers will explore the conversion of a variety of analogs (1) to the highly toxic chemical warfare agent, mustard gas (2), to less toxic derivatives using well-known organometallic carbonylation (Equation 1) and hydroformylation reactions (Equation 2).

Uruthira Kalapathy (Interim Chair & Assoc. Prof. /Analytical Chemistry).

Research efforts focus on silica based adsorbents in FTIR applications. Phenolic compounds and plant materials are analyzed using HPLC, NMR and GC-MS.

Anthony Rizzuti (Assoc. Prof./Geology/Environmental Science).

Research efforts focus on utilizing peats (organic-rich soils), peat-containing wetlands, and agricultural industry by-products as remediators of various environmental contaminants. The remediation occurs physically, chemically, or microbiologically. Instruments such as GC/MS, AAS, FTIR, HPLC, and UV-Vis are utilized to determine the remediation capacities of these products (peats, peat-containing wetlands, and agricultural industry by-products).

Nick Panasik (Assoc. Prof of Chemistry and Biology/Molecular Biology)

The eight stranded a/ b barrel protein fold is the largest family of protein structures (representing at least 10% of all known protein structures) and has the widest range of enzyme functions. My research focuses on elucidating the structural basis for folding specificity and thermodynamic stability in this class of enzymes and the future application of those principles in protein design. Specifically, I use random PCR mutagenesis to create a library of genetic variants for a variety of enzymes including beta-galactosidase. These variants are placed in an expression host that is a beta-galactosidase negative yet positive for the lactose transport genes. A temperature selection is applied. Using chromogenic substrates for screening, or nutrient restriction for selection, variants that display the selected phenotype (activity or stability at higher or lower temperature) can be selected. These variants are subjected to future rounds of mutagenesis and selection until variants with dramatically different enzymatic properties are produced. Using multiple successes from these “Directed Evolution” experiments, coupled with careful analysis of structure, patterns of mutations begin to emerge. These patterns help us posit generalized, fold-specific, molecular mechanisms of protein structural adaptation to temperature. These principles are then tested using site directed mutagenesis and rational design.