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. This sensitivity limits the potential applications and shelf life of these molecules. At the same time, it provides insight into the adaptations that organisms use to survive in their environmental niches. The first aim of this project addresses the effect of these sequences on the structure, stability, and salt tolerance of a particular halophilic enzyme, cysteinyl-tRNA synthetase, using site-directed mutagenesis and in vitro enzyme assays to assess the relationship between peptide sequence and function in this organism. The second aim of this project investigates the implications of environmental extremes on peptide structure, using multidimensional nuclear magnetic resonance. The intellectual merit of this project is that it lays the groundwork to understanding the strategies organisms that live in extreme conditions employ to remain viable in their unique environments. The broader impacts of this work is that it is conducted in Idaho, which is both an underprivileged state in terms of education and research funding, and yet is also home to large Hispanic and Native American populations; Idaho State University has large numbers of students from both of these ethnic groups. As a female scientist, the principal investigator will use her lab as to promote participation of women in science, at both the undergraduate and graduate levels.
