Office: Physical Science Complex, 356
Ph.D. Biological Chemistry, University of Pennsylvania – 1998
Research area: Biochemistry, Structural Biology, Microbiology
Student experience required for research: BIOL 101, 102, enrolled in 206; CHEM 111,112, enrolled in 301, 302
Student experience gained from research: Enzyme assays with non-traditional enzymes, molecular biology methods, microbiological methods, structural biology instrumentation, bioinformatics, and model building.
Ideal preparation for: Preparation for Professional schools- especially Graduate and Medical school, and Biotechnology and Pharmacology industries
My 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. My 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 37oC, 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.
"Catalysis by the second class of tRNA(m1G37) methyltransferase requires a conserved proline," T. Christian, C. Evilia, Y.M. Hou, Biochemistry 45, 7463-7, 2006.
"Acquisition of an insertion peptide for efficient aminoacylation by a halophile tRNA synthetase," C. Evilia, Y.M. Hou Biochemistry 45, 6835-45, 2006.
"Distinct Evolution of tRNA(m1G37) Methyltransferase," T. Christian, C. Evilia, S. Williams, and Y.-M. Hou, Journal of Molecular Biology 339, 707-719, 2004.
"Aminoacylation of an Unusual tRNACys from an Extreme Halophile," C. Evilia, X. Ming, S. DasSarma, and Y.-M. Hou, RNA 9, 794-801, 2003.
"The Archaeal Prolyl-Cysteinyl-tRNA Synthetase is Associated with a Multifunction Protein: Implication for a Multi-Synthetase Complex in Archaea," R. S. A. Lipman, O. Vitseva, C. Evilia, and Y.-M. Hou, Biochemistry 42, 7487-7496, 2003.
"Alternative Design of a tRNA Core for Aminoacylation," T. Christian, R. S. A. Lipman, C. Evilia, and Y-M. Hou, Journal of Molecular Biology 303, 503-514, 2001.