Caryn Evilia, Ph.D.
Associate Professor of Biochemistry
- (208) 282-3291
- Gale Life Sciences Bldg, Rm 431
The Evilia Lab
extremophiles, protein structure, adaptation, protein evolution, halophiles, extreme salinity
- Postdoctoral Fellow, 1999 - 2006, Thomas Jefferson University, Philadelphia, Pennsylvania
- Ph. D. Chemistry, 1998, University of Pennsylvania, Philadelphia, Pennsylvania.
- B.S. Microbiology, 1991, University of Massachusetts, Amherst, MA.
Dr. Evilia's research program is concerned with the effects of extreme conditions on proteins and nucleic acids, and on the structural adaptations organisms that live in these conditions have evolved to thrive in their environment. Her lab will study these factors through a combination of experimental and computational biochemistry, structural biology, and ultimately, genetic experimentation with archaebacteria.
Proteins and nucleic acids are very sensitive to their chemical and physical surroundings. Like the organisms from which they are isolated, these molecules tend to function and remain stable over a relatively narrow range of environmental conditions such as temperature, pH, salinity, and pressure.
What those narrow conditions are, however, can vary widely. Most organisms grow best at about 37 oC, under one atmosphere of pressure, with less than 0.2 M salt. But many archaebacteria do not; some grow in hot springs, for instance, or in hypersaline environments (such as the Great Salt Lake). These organisms must have evolved mechanisms to maintain the structural integrity of their proteins, nucleic acids, and membranes under these conditions, because human proteins, for instance, rapidly denature or lose activity when subjected to them.
Dr. Evilia's interest in archaebacteria started as an undergraduate microbiology major at the University of Massachusetts, Amherst, in the lab of Dr. Shiladitya DasSarama, where she investigated the potential for GC-rich promoter sequences to adopt alternative DNA structures. She continued her work on DNA structure as a doctoral candidate in chemistry at the University of Pennsylvania. As a postdoctoral researcher in Dr. Ya-Ming Hou's group at Thomas Jefferson University, she shifted her focus to proteins, investigating the peptide sequence adaptations organisms adopt to cope with extreme environments.
- BIOL 445/545 Biochemistry I (Fall 2006)
- BIOL 447/547 Biochemistry II (Spring 2007)
- BIOL 491/492 Senior Seminar (Spring 2007)
T. Christian, C. Evilia, Y.M. Hou (2006). Catalysis by the second class of tRNA(m 1G37) methyl transferase requires a conserved proline. Biochemistry 45, 7463-73.
C. Evilia, Y.M. Hou (2006). Acquisition of an insertion peptide for efficient aminoacylation by a halophile tRNA synthetase. Biochemistry 45, 6835-45.
T. Christian, C. Evilia, S. Williams, and Y.-M. Hou (2004). Distinct Evolution of tRNA(m 1G37) Methyltransferase. Journal of Molecular Biology339, 707-719.
C. Evilia, X. Ming, S. DasSarma, and Y.-M. Hou (2003). Aminoacylation of an Unusual tRNA Cys from an Extreme Halophile. RNA 9, 794-801.
R. S. A. Lipman, O. Vitseva, C. Evilia, and Y.-M. Hou (2003). The Archaeal Prolyl-Cysteinyl-tRNA Synthetase is Associated with a Multifunction Protein: Implication for a Multi-Synthetase Complex in Archaea. Biochemistry 42, 7487-7496.
T. Christian, R. S. A. Lipman, C. Evilia, and Y-M. Hou (2001). Alternative Design of a tRNA Core for Aminoacylation. Journal of Molecular Biology 303, 503-514