The design and engineering of protein catalysts that carry out rare or non-natural chemistry remains a challenging contemporary goal. However, enzymes are inherently limited by their chemical composition, i.e. the reagent pool that exists in nature and the amino acids and cofactors that form their physical and catalytic core. Because of this limitation, the majority of chemical transformations developed by synthetic chemists remain, at least to our knowledge, biologically inaccessible.
This lecture will describe recent developments in our efforts to develop low-molecular weight catalysts for asymmetric reactions. Over time, our view of asymmetry has ebbed and flowed, with foci on enantioselectivity, site-selectivity and chemoselectivity. In most of our current work, we are studying issues of enantioselectivity as a prelude to extrapolation of catalysis concepts to more complex stereochemical settings where multiple issues are presented in a singular substrate. Moreover, we continuously examine an interplay between screening of catalyst libraries and more hypothesis-dri
Imaging tools have revolutionized our understanding of living systems by enabling researchers to “peer” into tissues and cells and visualize biological features in real time. While powerful, these probes have been largely confined to monitoring cellular behaviors on a microscopic level. Visualizing cellular interactions and functions across larger spatial scales—including those involved in cell migration to distant tissues, immunosurveillance, and other biological processes—remains a daunting task. My research group is developing general toolsets to image such macroscopic
Solution and solid-state NMR facility for biomolecule and chemical characterization
Designed to simplify the process of finding local research technology solutions
I will present recent work from my lab on the development and applications of magic-angle spinning solid-state nuclear magnetic resonance (NMR) techniques toward the structural and dynamic analysis of supramolecular protein and protein-DNA assemblies.
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