The largest general area of interest in the Chemistry Department is that of biological chemistry, reflecting not only its academic and society importance, but the high level of success of faculty in this focus area in gaining both wide recognition and strong external funding. Due to the particularly interdisciplinary nature of the field, research in this area spans a wide variety of systems and approaches. Research projects focus on understanding membrane proteins, redox active enzymes, enzymes involved in transcription and translation, and the chemical principles which govern macromolecules. Projects aim to clarify the molecular detail which underlies active site catalysis, mechanisms in transmembrane signaling, and principles, structure, and mechanisms in protein folding and in macromolecular interactions. In the study of these systems, most groups combine tools from a variety of subdisciplines in chemistry and biology, sharing expertise and collaboration with numerous other groups on campus and around the world.

To understand the chemistry of biological macromolecules better, some groups design and synthesize inorganic and organic models of protein recognition or active sites, in order to test structural and mechanistic models derived directly or indirectly from biological systems. Others prepare synthetic DNA and RNA containing simple functional group substitutions to probe contacts in protein-nucleic acid interactions, while still others use synthetic peptides as model systems. Toward the same end, several groups also exploit the very powerful tools of molecular biology to prepare mutant proteins with perturbed active sites or to introduce specific probes of structure and function. Most labs combine
a variety of these approaches in their studies.

The research groups in biological chemistry use a variety of cutting edge chemical and biophysical tools. Newly emerging techniques in both solution and solid-state NMR provide information about structure and dynamics in macromolecules. EPR and EXAFS spectroscopy are used to focus on the local electronic environment at metalloenzyme active sites. Kinetic analysis is used to probe processes as diverse as nucleic acid chemistry and hydrogen-atom transfer catalysis in biological sysems. Fluorescence and circular dichroism measurements provide both local and global information on macromolecular conformation and stability. To complement these approaches, titration and scanning microcalorimetry measurements provide an understanding of the thermodynamics of macro-molecular interactions, while kinetic stopped flow and quench flow studies unravel complex mechanisms. Protein structure analysis by crystallographic, spectroscopic, and computational analysis is a major thrust area in our department and in closely allied departments such as Biochemistry & Molecular Biology. Students working in any of these labs can gain experience in a wide variety of approaches, developing the flexibility necessary to compete in the rapidly evolving field of biological chemistry.

The biological chemists are engaged in several interdepartmental research and training programs. Notable among these are the campus' interdisciplinary graduate program in Molecular and Cellular Biology, and the NIH-sponsored Training Program at the Chemistry-Biology Interface (directed by Prof. Lynmarie Thompson of our department).

For participating faculty see Research Matrix.