Sharon J. Nieter Burgmayer, W. Alton Jones Professor of Chemistry
Inorganic and Bioinorganic Chemistry
Ph. D. University of North Carolina, Chapel Hill
Park 289 || firstname.lastname@example.org || 610-526-5106
Research in the Burgmayer labs involves two areas of bioinorganic chemistry. One project is focused on modeling the catalytic site of the molybdenum enzymes. These enzymes are widely distributed throughout Nature where they perform redox reactions critical to the health of organisms spanning bacteria to humans. The catalyltic unit—the molybdenum cofactor—has several redox active parts: the dithiolene, the pterin and the molydenum. The goal of this project is to understand how these three redox units affect catalytic function. A second project involves the study of ruthenium complexes that bind and can damage DNA. These projects involve both inorganic and organic syntheses, many of which are performed under inert atmosphere environments. Chemical reactivity is studied by spectroscopic analysis, such as FT-NMR, FT-IR, UV-vis, and fluorescence, and electrochemical characterization within the Bryn Mawr chemistry department. Certain projects require other techniques, such as structure determination by x-ray crystallography, EPR or MCD, that are accomplished through collaborations with researchers at other institutions.
Professor Francl is engaged in both developing new methods for studying chemical systems using computational approaches, as well as in the application of theoretical models to problems of interest in organic, inorganic and biological systems. One example is the [n]mobiusenes, condensed aromatic molecules which mimic Moebius strips. Larger molecules are less strained than their smaller counterparts, but all show a counterintuitive localization of the twist. One imagines that the molecule would be less strained if the twist were distributed evenly around the molecule. What is the impetus for the localization? What are the consequences for the molecular reactivity? The answers to these questions can be found by mixing computational chemistry with a dash of topology and a generous dollop of differential geometry. Professor Francl's research group is taking an interdisciplinary approach to this and related problems.
The research program in the Goldsmith labs combines the techniques of inorganic, physical and synthetic chemistry to develop and investigate novel transition metal complex-based nanostructures. Electrochemical and spectroscopic techniques are used to probe the interactions of transition metal complexes with surfaces and to develop applications including nanoelectronics and solar energy conversion. Bifunctional ligands are synthesized where the aromatic portion of each ligand has π-stacking interactions with carbon surfaces. Electrochemical techniques including cyclic voltammetry and the use of an electrochemical quartz crystal microbalance (EQCM) are used to study the thermodynamics, kinetics and dynamics of the adsorption process. Investigations of cobalt, rhodium adn iridium complexes are directed towards fabrication of electron relays for solar energy-based hydrogen production.
Our research interests stretch across the field of organic chemistry from traditional areas, such as synthetic reaction development and natural product synthesis to bioorganic chemistry, including enzyme inhibitor design, synthesis and testing. In all these fields, our primary laboratory activities involve organic synthesis or constructing molecules. There are currently two active projects in the group: indoleamine 2,3-dioxygenase (IDO) inhibitor design and synthesis and natural product synthesis with the sequential Birch reduction-allylation and Cope rearrangement. The ultimate goal of both projects is to develop new therapeutics for the treatment of a variety of ailments, most notably cancer and infectious diseases.
The research interests in teh Mallory group are mainly in four areas of organic chemistry: (1) organic photochemistry concerned primarily with the mechanism and the synthetic applicability of the photocyclization of cis- stilbenes to produce phenanthrenes; (2) the synthesis of solubilized "graphite ribbons", very large (nanoscale) members of the family of novel polycyclic aromatic molecules known as phenacenes, and the investigation of their properties; (3) the use of nuclear magnetic resonance (NMR) spectroscopy to probe for certain intramolecular interactions in organic molecules; and (4) solid-state studies in collaboration with Professor Peter A. Beckmann of the Department of Physics involving the use of Zeeman 1 H and 2 H relaxation measurements to study the rates of the intramolecular rotation of alkyl groups attached to aromatic rings to elucidate a detailed understanding of the intramolecular and intermolecular factors that contribute to the energy barriers for the rotation of some simple alkyl substituents in various crystalline aromatic compounds. .
Jason Schmink, Assistant Professor of Chemistry
Ph.D. University of Connecticut
Arriving July 2012!!
Jason received his B.S. from the University of Illinois in 2005 and in 2010 earned his PhD from the University of Connecticut (Advisor: Nicholas E. Leadbeater). After a postdoctoral fellowship at the University of Pennsylvania in collaboration with Merck & Co., Jason began his independent career at Bryn Mawr College in July 2012. The Schmink Research Group focuses their research on harnessing the power of transition metal catalysis to effect novel bond-forming events. Additionally, the Schmink Research Group utilizes high-throughput experimentation techniques to rapidly explore a vast expanse of new reaction space to develop these exciting new approaches in organometallic chemistry. This endeavor at Bryn Mawr is particularly exciting as it is one of only a handful of such centers in academia at any level and the lone example utilizing this cutting-edge technology at a predominantly undergraduate institution!
Professor White's research interests are in the area of RNA structure, stability, and protein binding. The goal of Professor White's research is to understand how irregular structural features, such as helical regions containing standard Watson-Crick base pairs as well as internal and hairpin loops, contribute to the thermodynamic stability of the RNA molecule and function as sites for protein recognition. Her group studies the messenger RNA for yeast ribosomal protein L30 (formerly called L32) and the L30 autoregulation system. The White group has verified the existence of two helices and has shown that the internal loop is the site of protein binding (Ref 2). Using a combinatorial approach they have shown that two GA sequences are required for protein binding (Ref 5). Thermal denaturation experiments have shown that the purines in the internal loop are responsible for the cooperativity of the transition to the completely single-stranded state (Ref. 1). The structure of the L30 RNA:protein complex has recently been determined by NMR and supports our biochemical data (Ref 7). Because the RNA:protein interface is unusually intimate, protein mutations are made to asses the thermodynamic contributions of the interface residues.