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Full-Text Articles in Chemistry
Nickel-Catalyzed Oxidative Decarboxylative (Hetero)Arylation Reactions, Aaron P. Honeycutt
Nickel-Catalyzed Oxidative Decarboxylative (Hetero)Arylation Reactions, Aaron P. Honeycutt
Graduate Theses, Dissertations, and Problem Reports
Transition-metal-catalyzed decarboxylative coupling reactions have gained considerable attention over the past decade as an efficient route to form heterobiaryls. However, current methods for oxidative decarboxylative (hetero)arylation with unactivated C-H bonds have been limited by poor substrate scope, control of regioselectivity, and chemospecificity. This thesis describes the development of a new nickel-catalyzed oxidative decarboxylative coupling (ODC) with unactivated C-H bonds. The first chapter discusses the development of the new nickel-catalyzed ODC reaction to enable the coupling of a N,N'-bidentate directing group with a broad scope of heteroaromatic carboxylates and ortho-substituted benzoates, a scope that has not been achieved in previous …
Integrating Microscale Enzyme And Lectin Reactions Using Nanogel Assisted Capillary Electrophoresis, Srikanth Gattu
Integrating Microscale Enzyme And Lectin Reactions Using Nanogel Assisted Capillary Electrophoresis, Srikanth Gattu
Graduate Theses, Dissertations, and Problem Reports
Protein glycosylation is one of the most prevalent post-translational modifications which plays an important role in determining the structure, stability, and function of proteins. Changes in glycosylation patterns are a hallmark of cancer and other diseases. Characterizing glycosylation is difficult because these structures vary in their linkage and monomer sequence, which gives rise to vast microheterogenity that could affect the function of the molecule. A novel method using capillary gel electrophoresis by integrating microscale enzymes and lectin reactions in the capillary was developed to verify glycan structure by analyzing monosaccharides. Capillary electrophoresis (CE) improves upon conventional methods of glycan structure …