Lisa Bergeron.

Post-Doctorate Researcher
University of California, Berkeley

Ph.D. Chemical Engineering, 2008
University of California, BerkeleyB.S. Chemical Engineering, 2003
University of Houston

Office Location: 497A Tan Hall
Office Telephone: 510-643-8340
Office Fax: 510-643-1228

Molecular Chaperones and Extremophiles

The conditions in which an enzyme remains stable are not only of great importance in both pharmaceutical and chemical industries, but also could hold amazing possibilities for environmental, agricultural, and medical fields. For this reason, we seek to understand the means by which enzymes remain active, specifically to examine protein stability in the presence of molecular chaperones. We are interested in the effects of chaperones on enzyme stability to potentially prevent misfolding and aggregate formation under stress. We will explore the effect of stress-induced chaperones isolated from the hyperthermophilic archaeon Methanococcus jannaschii on the enzyme’s ability to perform. This may provide us with opportunities for the enhancement of enzyme stability, allowing us to expand the range of conditions in which an enzyme can function.

Bergeron LM, Tokatlian T, Gomez L, Clark DS, “Redirecting the inactivation pathway of penicillin amidase and increasing amoxicillin production via a thermophilic molecular chaperone”, Biotechnol & Bioeng. 2008.

L.M. Bergeron, C. Lee, D.S. Clark, “Identification of a critical chaperoning region on an archaeal recombinant thermosome,” Biochem Biophys. Res. Commun. 2008 369: 707-711.

L.M. Bergeron, C. Lee, T. Tokatlian, V. Höllrigl, and D.S. Clark, “Chaperone Function in Organic Co-solvents: Experimental Characterization and Modeling of a Hyperthermophilic Chaperone Subunit from Methanocaldococcus jannaschii,” Biochim. Biophys. Acta, 2008 Feb; 1784(2): 368-78.

Lisa Bergeron, Luis F. Filobelo, Oleg Galkin, and Peter G. Vekilov, “Thermodynamics of the Hydrophobicity in Crystallization of Insulin” Biophys. J. 2003 85: 3935-3942.