Abstract by Jordan Tretbar
Chemistry and Biochemistry
Nature has set an incredibly high standard when it comes to selective and efficient complex chemical processes that accomplish very specific purposes. Enzymes are a major component of these chemical processes and are responsible for such incredibly selective and efficient reactions. In an attempt to recreate such selectivity, the Michaelis laboratory is designing small helical peptides that mimic the reactivity and selectivity of enzymes. I have been researching and synthesizing different types of non-water soluble helical peptides in an attempt to develop peptide crystals for XRD analysis. I have recently begun my own research into new crystallization methods of these non-water soluble peptides. Crystallizing methods are relatively difficult due to there being limited resources available. As I develop these peptide crystals, my goal is to learn more about the nature of how our enzymes are interacting with each other. We will also be able to validate our helical peptide structures. Developing peptide crystals to see how two catalysts are interacting will play an important role in how we develop bi-functional peptide catalysts in the future.