Investigations in Catalysis
REU Research Programs with Brandeis Faculty
Research programs span solution and solid-state reactions, homogeneous and heterogeneous catalysis and both covalent and noncovalent polymer formation. Our faculty employ cutting-edge techniques like single molecule experiments and ultra-high resolution time-resolved protein crystallography to investigate fundamental questions like the role of structural dynamics in protein function.
Li Deng (Chemistry):
Our research program focuses on the invention and development of new catalytic and selective reactions because of their fundamental importance to the future of chemistry and other branches of science studying molecular properties. Our approach involves the discovery and design of accessible catalysts for highly enantioselective asymmetric organic reactions of broad synthetic importance, the elucidation of the reaction mechanism and molecular recognition events underlying the catalytic activity and selectivity, and the illustration of their applications in the synthesis of chiral compounds of varying complexity.
Irving Epstein (PI; Chemistry):
The Epstein laboratory studies the unusual array of complex spatiotemporal patterns that arise when the oscillatory Belousov-Zhabotinsky reaction and other systems with highly nonlinear kinetics are run in a microemulsion. After learning how to make microemulsions and work with oscillating reactions, the student will explore how changing the surfactant and oil compositions can affect the kinetics and the patterns formed in such systems. As the student becomes more independent, he/she will have the opportunity to investigate whether these novel spatial patterns can be used to catalyze the formation of new materials.
Bruce Foxman (Chemistry):
The Foxman examines the highly chemo- and stereospecific reactions which occur when a set of molecules is assembled in a favorable orientation in a crystal. Students will learn the techniques of X-ray structure determination and principles of solid-state reactivity, as well as facile approaches to the preparation and reactant-product characterization of materials which undergo a solid-state reaction.
Anne Gershenson (Chemistry):
The Gershenson laboratory uses single molecule techniques to investigate protein folding problems. The serpin class of serine protease inhibitors operate by a unique mechanism that disrupts the protease active site. These inhibitors control many important physiological processes including blood coagulation and fibrinolysis. The student will investigate the role of protease stability in serpin function, determining the relative stabilities of several serine proteases that are inhibited by the serpin α1-proteinase inhibitor.
Lizbeth Hedstrom (co-PI; Biochemistry):
The Hedstrom laboratory is investigating the mechanism of enzyme catalysis. The student will join our effort to design and synthesize new drugs against Cryptosporidium parvum. This water-borne parasite is an important AIDS pathogen and potential biowarfare agent in the developed world and a major cause of diarrhea and malnutrition in the developing world.
Oleg Ozerov (Chemistry):
The Ozerov laboratory is investigating the selectivity among oxidative addition of C-H vs. C-heteroatom bonds to complexes of iridium and rhodium that are supported by PNP “pincer” ligands. The student will explore a new subset, the competition between oxidative addition of C-H vs. C-O and C-S bonds, while becoming competent in the inert atmosphere experimental techniques and in the characterization methods such as NMR, IR, GC-MS.
Gregory Petsko/Dagmar Ringe (Biochemistry/Chemistry):
The Petsko and Ringe laboratories are developing a model system to study the origin, control and integration of new metabolic pathways and will utilize this system to understand the factors that govern the evolution of such pathways, to develop new ways of modeling them effectively, and to understand how they influence – and are influenced by – the core pathways already present in the organism. The student will characterize how a transplanted metabolic pathway operates and how an organism adapts to the presence of the new pathway.
Thomas Pochapsky (Chemistry):
The Pochapsky laboratory is trying to understand the origins of metal-dependent activity in acireductone dioxygenase (ARD). This enzyme shows different activities with the same substrates depending upon the metal bound in the active site. The project currently involves two undergraduates who are making mutations in the metal binding site to determine the origin of metal selectivity and are performing a variety of enzymatic assays, substrate and inhibitor syntheses and structural (NMR and x-ray crystallography) work.
Barry Snider (Chemistry):
The Snider laboratory is engaged in developing new methods for natural product syntheses. Current targets include the antibiotic abyssomicin C, symbioimine, bisabosqual, epohelmins A and B, jenamidine, bohemamine, dictamnine, SB-311099, and Sch 642305. The student will work closely with senior graduate students developing new methods and applying them to one of these targets.