Undergraduate Research Opportunities
(Last updated 10/2008)
Undergraduate Research Coordinator:
  • John Stuehr
  • 207 Clapp Hall, 368-5099
Department Chair:
  • Mary D. Barkley
  • 202 Clapp Hall, 368-0602

Research Activities

Undergraduate chemistry majors are encouraged to participate in the Undergraduate Research Program. The student should consult with faculty members in the department and select one under whose guidance the student undertakes a specific research project. The student has the opportunity to join a research group, to work with faculty, graduate students, and research associates. Many such research projects have resulted in papers published in scientific journals and co-authored by undergraduate students. Please consult the individual faculty member for information on the research.

Undergraduate Research/Independent Study Courses

CHEM 397 Undergraduate Research (1-6). Independent research for candidates for honors in chemistry and other qualified students. Not open to graduate students. Prerequisite: consent of department.

CHEM 398. Undergraduate Research/Senior Capstone Project (3-6). Independent project within a research group in the chemistry department or, by approval, within a research group in another Case department. Arrangements should be made by consultation with the faculty member selected and the Senior Capstone Committee of the chemistry department. Open to all chemistry majors and other qualified students. Satisfies the research requirement for Honors in Chemistry. A written report and public oral presentation is required. (Approved Sages Capstone) Prereq: Consent of department.

Registration Permit

The Registration Permit for CHEM 397 Undergraduate Research must be signed. Please see the Undergraduate Handbook for full details and requirements.

Faculty Research Summaries
  • Professor Alfred B. Anderson
  • 228 Millis Science Center, 368-5044
  • Undergraduates who would like to work with a computer and apply quantum mechanics to problems of molecular structures and reactions. Quantum mechanics or chemistry 337 are prerequisites when space permits. Surface Science: The current research focus is on Low Pressure Diamond Growth Diamond surface structures and reaction mechanisms. Bulk electronic structure modification by doping. Electrochemistry Potential dependence of fundamentalelectrocatalytic reactions; focus on fuel cells.
  • Professor Mary Barkley
  • 202 Clapp Hall, 368-0602
  • Laser fluorescence spectroscopy; biophysical chemistry; proteins, DNA, and RNA; HIV and Hepatitis C viral enzymes.
  • Associate Professor Clemens Burda
  • 225 B Millis Science Center, 368-5918
  • Research in the Center of Chemical Dynamics and Nanomaterials Research directed by Prof. Burda involves collaboration with several national Laboratories on nanomaterials research. Motivated Undergraduates can be integrated in the ongoing research on novel and functional nanomaterials. Laboratory training includes synthesis of nanomaterials, bioconjugation techniques and fine-tuning of nanomaterials by adjusting the chemistry of more complex systems. We prepare nanomaterials with new electronic, magnetic, and optical properties with applications in catalysis, photovoltaics, micro/nano-electronics, and bio-medicine. A wide range of state-of-the-art techniques is available for characterization on campus . Synthesis and opto-electronic characterization can be performed in our laboratory. The laser facility allows to measure chemical reaction dynamics on a femtosecond (10-15 sec) time-scale.
  • Associate Professor James D. Burgess
  • 225A Millis Science Center, 368-4490
  • Research focuses on immobilizing biological structures on electrode surfaces for sensing. Energetic students can gain experience in electrochemistry and surface science. Some characterizations of biosensor performance are well suited for the beginning scientists.
  • Professor Robert C. Dunbar
  • G22A Millis Science Center, 368-3712
  • The group's research focuses on chemistry of gas-phase ions using mass spectrometry, particularly the technique of Fourier-transform mass spectrometry (FTMS). We combine these experimental studies with quantum calculations of the same reactions that we observe in the mass spectrometer. Both experiments and computations have provided successful topics for undergraduate activities in the group. FTMS studies of metal ion binding to amino acids, aromatic hydrocarbons, and other interesting molecules. Interstellar chemical reactions of metal ions combining with known components of interstellar clouds, modeled by experiments in the mass spectrometer at very low pressure, and by calculations and simulations. Quantum chemical calculations of complexation of transition metals with curved and planar graphitic sheets and extended aromatic hydrocarbons, as well as biologically interesting model sites.
  • Assistant Professor Thomas G. Gray
  • 212 Clapp Hall, 368-0991
  • Research efforts in the Gray group focus on the transition elements, especially on metal-atom clusters, and on the opportunities they present for groundbreaking chemistry. The work emphasizes synthesis, but also relies upon spectroscopic and crystallographic characterization of new compounds. Principle research topics include biomineralization and nanoscience, and new applications of cluster chemistry are common to both. One project examines the binding interactions of the biological peptide phytochelatin with well-defined metalloclusters, in an effort to understand peptide-induced mineralization of cadmium sulfide in plants. Additional efforts focus on preparing infinite clusters (metallocluster nanorods), with potential applications to nanoelectronics and molecular devices.
  • Professor Malcolm E. Kenney
  • 432 Millis Science Center, 368-3739
  • Organosilicon Compounds. Some of our studies deal with the synthesis and characterization of organosilicon compounds. The silicones being sought have structures which are new and can be expected to have properties which are desirable and unique. Macrocyclic Complexes. We are also working on metal phthalocyanines (compounds which are closely related to metal porphyrins). The metal phthalocyanine work has as a goal the synthesis and characterization of compounds that can be used as drugs in cancer therapy and for purging donated blood of HIV and hepatitis viruses. Particular attention is being given to making compounds that have the needed physical properties.
  • Associate Professor Irene Lee
  • G24A Millis Science Center, 368-6001
  • Our research focuses primarily on the application of biochemical techniques to elucidate the chemistry of the biological processes associated with protease. Instruments such as the fluorimeter and spectrophotmometer are employed in enzyme kinetics experiments. Standard procedures include solid phase peptide synthesis, cloning, PCR, and preparing and running electrophoretic gels.
  • Professor Anthony J. Pearson
  • 433A Millis Science Center, 368-5920
  • Undergraduate research participants are welcome to join our group and gain experience with a variety of techniques and methods in organic and organometallic chemistry. Our major interests are in the applications of organometallic complexes in the solution of difficult organic synthesis problems. This has involved us in a number of projects aimed at the total synthesis of natural products, one example being our current approach to the total synthesis of the complex glycopeptide antibiotics ristocetin A and vancomycin, which use transition metal-promoted aryl ether formation developed in our laboratories.
  • Professor John D. Protasiewicz
  • 418A Millis Science Center, 368-5060
  • Specific projects center around the study of metal catalyzed atom and group transfer reactions (such as oxo, nitrene, phosphido, carbene, hydride, and other similar moieties). Understanding the details is key to the optimization of current technologies and for the rational design of new bond forming reactions. Mechanistic studies can identify potential intermediates; synthetic and structural studies yield important information about the bonding in intermediate and precursor species. Our labs house the departmental X-ray facility; thus we routinely use single crystal diffraction studies to uncover the molecular details of "never seen before" complexes and relate these structural data to observed reactivity patterns.
  • Professor Robert G. Salomon
  • 212 Millis Science Center, 368-2592
  • Enthusiastic undergraduates eager to learn laboratory chemistry and committed to invest reasonable time and effort are always welcome in our group. Research projects involving one or more of the following areas are always available:
  • 1. Synthesis of medicinally useful and biologically important natural products.
  • 2. Mechanistic studies of organic reactions and biochemical pathways.
  • 3. Biological chemistry of lipids. Some of the techniques which may be learned include: analytical and preparative gas-liquid phase, high performance liquid, column, and thin-layer chromatography, gel electrophoresis, nuclear magnetic resonance, ultraviolet, and mass spectroscopy, immunoassay, liquid scintillation counting, advanced techniques of preparative organic chemistry.
  • Professor/Chair Lawrence M. Sayre
  • 411 Millis Science Center, 368-3704
  • Research in my group focuses on understanding reaction mechanisms that underlie selected problems in biochemistry. Three projects are currently being pursued:
  • Development of selective amine oxidase inhibitors. By combining chemical and enzymologic approaches, we are unraveling the mechanisms of enzymatic amine oxidations, in particular by the quinone-dependent copper amine oxidases. Current work focuses on the design, synthesis, and enzymologic evaluation of mechanism-based (suicide) inhibitors.
  • Metal-catalyzed reactions of molecular oxygen with organic substrates. We are investigating the potential of readily accessible metal complexes to catalyze selective oxidation and/or oxygenation reactions as a function of substrate-metal coordination. These studies will help unravel the mechanisms of the various biological metalloenzymes and pathophysiologic processes associated with the role of copper and iron in oxidative stress.
  • Pathological posttranslational oxidative modification of proteins in degenerative disease. Modification of proteins during conditions of oxidative stress can result in abnormal protein function and contribute to diseases such as atherosclerosis and Alzheimer disease. We are using a combination of chemical model studies, immunochemical analysis, and mass spectrometry to investigate the structural aspects of these protein modifications and the mechanisms that explain them.
  • Professor Daniel A. Scherson
  • 227 Millis Science Center, 368-5186
  • Electrocatalysis. In Situ Spectroelectrochemical Techniques. In Situ and Ex situ Spectroscopic Techniques for the Study of solid-liquid Interfaces.
  • Assistant Professor Gregory P. Tochtrop
  • 410A Millis Science Center, 368-2351
  • Professor Michael G. Zagorski
  • G27A Millis Science Center, 368-3706
  • Protein Misfolding and Human Disease
  • Undergraduate students who are eager to learn state-of-the-art nuclear magnetic resonance (NMR), peptide synthesis and purification, as well as other analytical techniques for protein structure characterization are encouraged to join my group. The major research projects focus on studying the dynamics and structures of proteins in solution. Frequent collaborations with scientists in the School of Medicine are fundamental to the long-term goals of the group's research, which is the understanding the relationship between protein misfolding and human disease. Current research efforts are focused on proteins that are important pathological features in Alzheimer's disease, including the Aß peptide, the ABri peptide of Familial British dementia, serum amyloid A, a-synuclein, the human prion protein, and a 43-residue peptide segment that includes the membrane-spanning region of the amyloid precursor protein.
  • The Zagorski group has primarily focused their efforts with the Aß peptide, which produces amyloid plaques in Alzheimer's disease. The Aß pathologic effects are related to the formation of insoluble aggregates dominated by ß-sheet structures. To gain physical insight into the various possibilities, the Zagorski group has been systematically examining the structures and stabilities of the 40-residue Aß (1-40) and the 42-residue Aß(1-42) peptides as a function of pH, solvent polarity, and the presence of a membrane-like surface. In fact, they are still the only group that has successfully applied high-resolution NMR methods to study the structure and aggregational properties of the full length (native) Aß peptides in solution, as monomers, the earliest stage before it begins to aggregate as amyloid.