The synthesis of complex organic molecules used in the formation of many diverse products ranging from plastics to medicine will commonly require the presence of a substance which does not directly participate in the chemical reaction, but instead helps initiate or aid the rate of the reaction. These complexes are referred to as catalysts and consist of a molecule composed of both metallic and organic atoms/molecules. The goal of this study is to help produce a more viable and efficient iridium catalyst, in order to improve the sustainability of reactions that require an organometallic catalyst, such as C-H activation reactions. To improve catalytic capabilities, the chemical composition will be altered by attaching, or removing organic molecules from the Iridium center. To perform this reaction we will be following a previously published multistep synthesis procedure. This will require us to synthesize and purify various organic compounds which will then be used in a multistep reaction to eventually produce (1-tert-Butyl-3-(2-(2-acetamido)-3-phenylalanine methyl ester) imidazol-2-ylidene) Ir(iii) bromide. All compounds synthesized in the lab will be analyzed through NMR, and TLC plates, as well as purified through the use of column chromatography. At the moment we have successfully synthesized and purified the first 3 organic compounds in the multistep reaction, and will use these products to continue the overall reaction mechanism.

The application of enzymatic degradation to polysaccharides creates a useful and intuitive approach to creating biofuels. By making use of single domain and multi-domain enzymes called glycoside hydrolases, polysaccharides can be easily broken down. Using multi-domain enzymes may prove more efficient than using single domain enzymes due to the multiple activity nature of multi-domain enzymes allowing for synergetic activities to occur. Through previous computational approaches, we were able to find several potential glycoside hydrolases with potential cellulase or xylanase activity. Initial biochemical experiments resulted in showing enzymatic activity in two of the five initially predicted putative enzymes. Our goal is to better understand the architecture of putative enzymes. To do this, we utilized computational programs such as SWISS-MODEL, Robetta, and DEMO to model both single domain and multi-domain structures. The results gathered from the computations usually adopt structures of domains based on sequence homology-this methodology resulted in many structures being predicted for each domain. To further understand the structures of domains, comparisons were made between the single domain and multi-domain structure predictions in one program and different programs. Predictions for multi-domain structures showed that single domain structures linked together in an assembly fashion. The results found for both types of domain structures may help design multi-domain structures for glycoside hydrolases that are able to propel biofuel production in the future.

Just in the United States, plants are responsible for attacking fifty thousand different pathogens including fungi, viruses, bacteria, and nematodes. [1] In recent studies, Capsella burse-pastrois has shown to contain a wide range of chemicals including flavonoids, alkaloids, polypeptides, choline, acetylcholine, histamine, tyramine, fatty acids, sterold, organic acids, amino acids, sulforaphane, vitamins, and many other compounds. [2] Along with this, it has been proven that Capsella burse-pastoris has a long history of having antimicrobial activity by acting as an astringent specifically used for treating excessive uterine bleeding. Physicians have used shepherd's purse to treat hematuria and menorrhagia. Alon side the beneficial aspect of this plant acting as an anti-bleeding and anti-inflammatory -indications of medicinal properties of anticancer have been investigated but maintain a literature gap in conducting all possible anti-cancer research variables in Capsella burse-pastrois. [3]