Facilities and Instruments

The Shepherd University chemistry program occupies seven state-of the-art chemical laboratories, a computer laboratory, and several lecture rooms on the top floor of the nine-million dollar Robert C. Byrd Science Center. The Department is very well equipped with modern instrumentation. Majors in chemistry will routinely use all instruments throughout their academic careers. Listed below are the general uses of each of our major instruments followed by typical uses by our students in laboratory experiments and research projects.

AAS is mainly used for the determination of trace metals.

Analytical chemistry students have many uses for the AAS's. For example, they study the Fe, Ca, Mg and Cu content of food and determine the composition of alloys. Research students have utilized the AAS's for measurement of Cd, Fe, Cr, Mg, Zn, and Ni in landfill run-off and for the analysis of paint pigments.

NMR is the most powerful method for molecular structure determination. Our NMR is capable of one- and two-dimensional spectra. NMR is often used for kinetic studies.

Students in Organic Chemistry Lab use H-1 and C-13 NMR for the verification of the structure of the products that they prepare in lab. Organic students also use NMR to study hydrogen-deuterium exchange rates.

FT-IR is used to study the vibrations of molecules. This information can help to identify the type of molecule. One of our instruments is equipped with a computerized library of spectra and with an attenuated total reflectance accessory.

Students employ the FTIR for the identification and characterization of organic compounds synthesized in our laboratories such as aspirin, the food additive anethole, and the artificial sweetener dulcin, or to compare the experimental vibrational frequency of the C=O bond with theoretically calculated values.
Physical chemistry students use FT-IR to analyze the structure of small gas-phase molecules.

Gas chromatographs are used to determine the purity of volatile substances. In ideal cases one peak is observed for each component of a mixture. The GS-MS is especially powerful because the mass spectrum obtained aids in the identification of the components of a mixture. All GC's are commonly employed for quantitative analysis.

These instruments are part of many experiments performed by students in Organic Chemistry and Instrumental Analysis Labs. In student research, the GC-MS has been employed for the identification of sterols from plants, for the analysis of hydrocarbon residues left behind after a suspected arson attack, and for the determination of the essential oils in various food products.

HPLC's are used to examine the purity of almost any substance that can be dissolved. As in GC, in ideal cases one peak is observed for each component of a mixture. Many more substances can be studied by HPLC than by GC.

Students utilize the HPLC instruments for many projects, including the separation of analgesic drug mixtures and the measurement of caffeine or aspartame in soft drinks. Student research projects include assaying of ergosterol and other sterols from plant samples, measurement of the photoproducts of Vitamin D precursors, and evaluation of the efficiencies of various extraction methodologies for essential oils derived from food products.

UV-visible instruments are used for quantitative analysis of both organic molecules and metal ions in solution. Our department has a double-beam scanning instrument and a diode-array instrument.

Students perform labs such as the determination of the UV-screening properties of sunscreens, the kinetics of dimerization in a Diels-Alder reaction, and the determination of metal ions in complex mixtures. In Physical Chemistry Lab students study the correlation between molecular structure and the color of a substance.

Separation of amino acids and proteins.

Electrophoresis plays an important part in Biochemistry Lab. Projects include separation of proteins from serum and other biological sources, determination of the molecular weight of proteins, and the determination of the purity of enzymes.