“Among the Best in the World!”
- 9th in 2006 US News and World Report rankings.
- The 1997 Nobel Prize in Chemistry was awarded to faculty member, Paul Boyer.
- Six of our faculty are members of the National Academy of Sciences
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Latest News
has been elected to the National Academy of Sciences. For more information see the
National Academies press release
Seaborg Symposium 2012
Friday, Dec. 7, 2012
Honoring Harold Varmus
1989 Nobel Laureate &
Director of the National Cancer Institute
More >>
Professor James U. Bowie
Professor James Bowie and his group are fascinated by protein structure, folding and stabilization. This interest has led them into three main areas: (1) learning how membrane proteins fold and how they can be stabilized; (2) the structures and biological functions of a biological polymer they discovered, that is formed by a very common protein module called a SAM domain; (3) developing and stabilizing enzyme pathways for the production of biofuels.
Professor Guillaume F. Chanfreau
Professor Guillaume Chanfreau’s laboratory is interested in gene expression regulation in eukaryotic cells, with a particular emphasis on post-transcriptional steps. Within this large field, they are focusing on understanding how cells degrade RNAs that arise from malfunctions in gene expression pathways (“RNA surveillance”). In particular, they are analyzing the functions of the double-stranded RNA endonuclease RNase III and of the nonsense-mediated decay pathway in RNA surveillance, and how these enzymes regulate gene expression.
Professor Catherine F. Clarke
Professor Catherine Clarke and the Clarke lab study the biosynthesis and functional roles of coenzyme Q (ubiquinone or Q). Q functions in mitochondrial respiratory electron transport and as a lipid soluble antioxidant. The group is using the yeast Saccharomyces cerevisiae (bakers yeast) to elucidate the biosynthetic metabolism of Q. Their experimental approach employs a combination of molecular genetics, lipid chemistry and biochemistry to delineate the steps responsible for Q biosynthesis.
Professor Steven G. Clarke
A major interest of Professor Steven Clarke’s Laboratory is understanding the biochemistry of the aging process. The group is particularly interested in the generation of age-damaged proteins by spontaneous chemical reactions and the physiological role of cellular enzymes that can reverse at least some portion of the damage. They have focused their efforts on the degradation of aspartic acid and asparagine residues and the subsequent metabolism of their racemized and isomerized derivatives. The group is presently determining the biological role of protein methyltransferases that can initiate the conversion of D-aspartyl residues to the L-configuration as well as the conversion of isopeptide linkages to normal peptide bonds. Such “repair” reactions may greatly increase the useful lifetime of cellular proteins and may help insure organismal survival. View Professor Clarke’s YouTube Lecture
Professor Robert T. Clubb
Professor Robert Clubb investigates the molecular basis of bacterial pathogenesis. In particular, his group studies how microbes display and assemble cell wall attached surface proteins, and how they acquire essential nutrients from their host during infections. The group’s study could lead to creating new inhibitors of bacterial infections.
Professor Albert J. Courey
Professor Albert Courey and his group study the molecular basis of cell development. During embryogenesis, a cluster of apparently undifferentiated cells is transformed into an ordered array of differentiated tissues. Using Drosophila as a model system, his research group combines biochemical and genetic approaches to study the molecular basis of this amazing transformation. Essentially all the regulatory circuits they study are conserved throughout the animal kingdom. Therefore, their studies have important implications for human health and development.
Professor David S. Eisenberg
Professor David Eisenberg and his research group focus on protein interactions. In their experiments they study the structural basis for conversion of normal proteins to the amyloid state and conversion of prions to the infectious state. In bioinformatic work, they derive information on protein interactions from genomic and proteomic data, and design inhibitors of amyloid toxicity.
Professor Juli Feigon
Professor Julie Feigon and her research group study nucleic acid structure and specific recognition of nucleic acids by proteins. Her group focuses on determining the three-dimensional structures of DNA and RNA, and on investigating their interactions with various proteins and ligands, and to study nucleic acid folding.
Professor James W. Gober
Professor James Gober‘s group is interested in the mechanisms that couple cellular morphogenesis to gene expression. Early flagellar assembly events are required for the transcription of genes encoding structures that are assembled later in the flagellum. These same events are also required for normal cell division. The group is determining how factors that regulate gene expression and cell division monitor the assembly of the cellular structures.
Professor Wayne L. Hubbell
Professor Wayne Hubbell’s research is focused on understanding the relationship between the molecular structure of a protein and the conformational changes that control its function. Of particular interest are membrane proteins that behave as “molecular switches”, i.e., proteins whose structures are switched to an active state by a physical or chemical signal.
Professor Carla M. Koehler
Professor Carla Koehler and her research group encompass two major areas: Understanding the mechanism of protein import into mitochondria and determining the process by which defects in mitochondrial protein translocation lead to disease.
Professor Christopher J. Lee
Professor Christopher Lee‘s main area of research is in bioinformatics. His group studies 1) analysis of alternative splicing and genome evolution, 2) analysis of protein evolutionary pathways, and 3) development of a general framework for working with genomic data as an abstract graph database.
Professor James C. Liao
Professor James Liao and his group focus on metabolism, including its biochemistry, extension, and regulation. His group uses metabolic engineering,synthetic biology, and systems biology to construct microorganisms to produce next generation biofuels and to study the obesity problem in human. Their ultimate goal is to use biochemical methods to replace petroleum processing and to treat metabolic diseases.
Professor Joseph A. Loo
The research interests of Professor Loo’s group include the development and application of bioanalytical methods for the structural characterization of proteins and post-translational modifications, proteomics-based research, and the elucidation of disease. The composition and structure of noncovalently-bound protein-protein and protein-ligand interactions are studied by electrospray ionization mass spectrometry and ion mobility.
Professor Harold G. Martinson
Professor Harold Martinson’s group is interested in how the genes of organisms transmit their information to the cellular biosynthetic machinery. The group is especially interested in how this is accomplished in the most complex of organisms—eukaryotes in general, but especially in mammals. RNA polymerase II is the enzyme charged with initiating the transfer of information from the DNA in the nucleus to the cell cytoplasm via RNA. Amazingly, RNA polymerase not only carries out the intricate task of precisely transcribing the DNA, but it also oversees the elaborate network of events involved in processing the RNA that it makes. The group’s focus is on the functional interactions of the transcriptional machinery with the machineries responsible for cleavage and polyadenylation and for splicing.
Professor Sabeeha S. Merchant
The Merchant research program focuses on trace metal metabolism using Chlamydomonas as a reference organism. The group uses a combination of classical genetics, genomics and biochemistry to discover mechanisms of trace metal homeostasis in Chlamydomonas, especially mechanisms for reducing the quota or for recycling in situations of deficiency.
Professor Margot E. Quinlan
Professor Margot Quinlan and her group use biochemistry, microscopy and genetic approaches to study regulation of the actin cytoskeleton. The group is currently focused on Spire (Spir) and Cappuccino (Capu), two proteins that collaborate to build an actin network essential for early body axis development. Combining an in vitro understanding of the mechanism of Spir and Capu with in vivo studies of polar cells will provide insight into how the actin cytoskeleton is regulated and a broader understanding of cell polarity.
Professor Emil Reisler
Professor Emil Reisler’s group investigates cell motility and force generation mechanism of actin, tubulin, and a family of motor proteins. The aim of these studies is to obtain a structural description of the mechanism of motion and force generation. At the cellular level, the group studies the function, interactions, and structural transitions of the assembled protein systems.
Professor Jorge Z. Torres
The Jorge Torres Lab investigates mitotic spindle formation during cell division and its misregulation in human diseases, especially cancer. The lab’s major focus is to understand how multiple mechanisms and enzymatic activities coordinate the formation of the mitotic microtubule spindle during cell division. The group uses human cell lines and in vitro systems along with a combination of approaches, including Biochemistry, Molecular Biology, Cell Biology, Chemical Biology and Microscopy to determine the mechanism of action of these proteins.
Professor Joan S. Valentine
Professor Joan Valentine’s research group focuses on the role of metal ions in biological oxidation, including oxidative stress, and in naturally occurring antioxidant systems. It has three central themes: (1) biological studies of CuZnSOD in vivo, (2) coordination complexes as models for catalysts involved in biological oxidation, and (3) biophysical characterization of isolated copper-zinc and manganese superoxide dismutase ((CuZnSOD and MnSOD). Recent work on CuZnSOD proteins has focused on the role of mutations in CuZnSOD in causing familial amyotrophic lateral sclerosis (ALS, Lou Gehrig’s disease).
Professor Richard L. Weiss
Professor Richard Weiss’ research focus is to understand the role of compartmentation of enzymes and metabolites in biological regulation. The organellar localization of metabolic pathways requires considerable expenditure of metabolic energy for protein targeting, organelle assembly, and movement of substrates and products across intracellular membranes. Such expenditures must result in biological efficiencies commensurate with the investment of biological resources. Our hypothesis is that these compartmentation features play a significant role in the biology of the organism.
Professor Todd O. Yeates
Professor Todd Yeates and his group focus heavily on structural, computational, and synthetic biology aspects of chemistry. His emphasis is on supra-molecular protein assemblies and synthetically designed protein assemblies, and conducts research in computational genomics in order to infer protein function and to learn new cell biology.