barton photo

Jacqueline K. Barton
California Institute of Technology


Professor Barton has pioneered the application of transition metal complexes to probe recognition and reactions of double helical DNA. She has designed chiral metal complexes that recognize nucleic acid sites with specificities rivaling DNA-binding proteins. Most recently, her research group has designed bulky metalloinsertors as site-specific probes of DNA base mismatches. Barton has also carried out seminal studies to elucidate electron transfer chemistry mediated by the DNA double helix. This chemistry has since been applied in the development of DNA-based electrochemical sensors and is being explored in the context of long range signaling of oxidative damage and repair within the cell.

Carolyn R. Bertozzi
University of California, Berkeley


Prof. Bertozzi pioneered the field of bioorthogonal chemistry with the development of organic reactions that can be performed in living systems. Her group employs these chemistries for in vivo imaging and disease biomarker discovery, as well as for site-specific protein modification toward the development of hybrid chemical/biological therapeutics. As well, Prof. Bertozzi applies chemical tools toward the identification of targets for antibiotics, particularly against M. tuberculosis, and for integrating nanomaterials with biological systems.

Laura L. Kiessling
University of Wisconsin-Madison


Professor Kiessling’s group develops and implements synthetic methods to access biologically-active compounds for hypothesis-driven and discovery-driven research. The Kiessling lab utilizes synthetic natural products and natural product-like structures to probe cell surface receptor interactions, oligosaccharide biosynthesis, carbohydrate recognition, and glycoconjugate function. The Kiessling lab has also developed new strategies for peptide/protein synthesis that provide access to sequences with critical posttranslational modifications (e.g., glycosylation, tyrosine sulfation) that can be used to elucidate the biological roles of these modifications.

Harry B. Gray
California Institute of Technology


In work in the early 1960s at Columbia, Harry Gray developed ligand field theory to interpret the electronic structures and substitution reactions of metal complexes. After moving to Caltech in 1966, he began work in biological inorganic chemistry, focusing on the electronic structures and mechanisms of redox reactions of metalloroteins. In 1982 he and his students demonstrated that electrons can tunnel rapidly over long molecular distances through folded polypeptide structures; and, in the years following, he and J. R. Winkler developed laser flash-quench methods that opened the way for experimental investigations that have led to a deeper understanding of the mechanisms of electron flow through proteins that function in respiration and photosynthesis. In recent years he has turned his attention to one of the outstanding problems in 21st century science, the efficient and economical production of fuels and other molecules from solar-driven water splitting reactions.

Stephen J. Lippard
Massachusetts Institute of Technology


Professor Lippard studies biological interactions involving metal ions, focusing on reactions and physical and structural properties of metal complexes. Such complexes can be useful as cancer drugs and as models for the active sites of metalloproteins. Lippard is well known for his work on the mechanism of the anti-cancer drug cisplatin. His lab is currently working on designing more effective platinum anti-tumor agents. The Lippard group also determined the structure of the component proteins of methane monooxygenase, as well as the structures of the related hydroxylase enzymes from toluene/o-xylene monooxygenase and phenol hydroxylase. Lippard recently developed a fluorescent sensor that can monitors nitric oxide in living cells. Professor Lippard has also developed fluorescent and MRI sensors to detect and understand the roles of mobile zinc in the brain.

Roger Y. Tsien
University of California, San Diego


The overall goal of Professor Tsien’s laboratory is to gain a better understanding of signaling inside individual living cells, in neuronal networks, and in tumors. His group designs, synthesizes, and uses new molecules that detect or manipulate biochemical signals. The Tsien group builds both small synthetic molecules and genetically encoded macromolecules, which preferably work together in synergy. Tsien revolutionized much of molecular and cell biology with his work on the Green Fluorescent Protein (GFP), as it provided the first genetic means to encode strong visible fluorescence. The Tsien lab has also engineered chimeric fluorescent proteins that monitor important intracellular signals such as Ca2+, cyclic AMP, and cyclic GMP.