Search for dissertations about: "site-specific covalent modification"
Showing result 1 - 5 of 6 swedish dissertations containing the words site-specific covalent modification.
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1. Development of a covalent site-specific antibody labeling strategy by the use of photoactivable Z domains
Abstract : The joining of two molecular functions or the strategy of adding functions to proteins has been tremendously important for the development of proteins as tools in research and clinic. Depending on the intended application, there are a wide variety of functions that can be added to a proteins. READ MORE
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2. Catalysis and Site-Specific Modification of Glutathione Transferases Enabled by Rational Design
Abstract : This thesis describes the rational design of a novel enzyme, a thiolester hydrolase, derived from human glutathione transferase (GST) A1-1 by the introduction of a single histidine residue. The first section of the thesis describes the design and the determination of the reaction mechanism. READ MORE
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3. A Novel Route for Construction of Multipurpose Receptors through Chemical Modification of Glutathione Transferases
Abstract : This thesis describes how the human Alpha class glutathione transferase (GST) A1-1 can be reprogrammed either to function as a multipurpose biosensor for detection of small molecule analytes, or as a handle providing for more efficient protein purification.A novel, user-friendly, and efficient method for site-specific introduction of functional groups into the active site of hGST A1-1 is the platform for these achievements. READ MORE
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4. Selective protein functionalisation via enzymatic phosphocholination
Abstract : Proteins are the most abundant biomolecules within a cell and are involved in all biochemical cellular processes ultimately determining cellular function. Therefore, to develop a complete understanding of cellular processes, obtaining knowledge about protein function and interaction at a molecular level is critical. READ MORE
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5. Cellobiohydrolase I as a chiral sector
Abstract : The protein cellobiohydrolase I (CBH I) immobilized on silica particles has been used as a chiral selector in liquid chromatography (LC) and the free enzyme has served as a chiral complexing agent in the background electrolyte in capillary electrophoresis (CE) using the partial tilling technique.The CE systems were much more efficient and more solutes could be enantioseparated than in the LC systems. READ MORE