Mike Liszka.

Graduate Student
University of California, Berkeley

Ph.D. Chemical Engineering, 2012
University of California, Berkeley

B.S. Chemical Engineering, 2007
Purdue University

mliszka(AT)berkeley.edu
Office Location: 473A Tan Hall
Office Telephone: 510-643-8340
Office Fax: 510-643-1228


Non-Aqueous Enzyme Catalysis & Dynamics

The general goal of my research is to reveal links between motion, electrostatics and function in proteins, and to then use those links to engineer more active enzymes in organic solvents. I use as a model system a catalytic protein dissolved in organic solvents. Organic solvents provide a way to manipulate a protein’s physicochemical properties through dielectric, viscosity, and water content. Previous work with the enzyme subtilisin in organic solvents has shown that protein hydration and the presence of salts can dramatically influence catalytic activity; although, detailed structural, electronic, and dynamic data for these systems are still lacking. To fill this information gap, we use high resolution protein NMR to measure structural and dynamical properties of the protein under these unnatural conditions. Over the past few decades many surfactant centered techniques have been developed for solubilizing enzymes in solvents, thus making high resolution NMR possible. We utilize a system where the protein is ion-paired to a surfactant, in which the enzyme has no water shell, resulting in direct solvent contact. This system is ideal for studying solvent effects on structure and dynamics, and how these influence catalysis. My work also focuses on the effects of mutations on the dynamics and catalysis of organic- or mixed-phase enzymes. We use high throughput assays for screening catalytic activity of mutants in both the organic and aqueous phases. Through these mutants we should be able to identify concerted or individual-residue motions that are essential to catalysis.