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Showing result 1 - 5 of 18 swedish dissertations matching the above criteria.

2. 1. Catalysis and Site-Specific Modification of Glutathione Transferases Enabled by Rational Design

   Author : Sofia Håkansson Hederos; Lars Baltzer; Kerstin Broo; Linköpings universitet; []
   Keywords : TEKNIK OCH TEKNOLOGIER; ENGINEERING AND TECHNOLOGY; Catalysis; Glutathione Transferases; Rational design; Protein design; Site-specific modification; thiolester hydrolysis; Enzyme engineering; Enzymteknik;

   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

4. 2. Development of a covalent site-specific antibody labeling strategy by the use of photoactivable Z domains

   Author : Anna Konrad; Sophia Hober; Hjalmar Brismar; Patrik Samuelsson; KTH; []
   Keywords : antibody labeling; site-specific; covalent; SPPS; Z domain; BPA; SRA - Molecular Bioscience; SRA - Molekylär biovetenskap;

   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

5. 3. Ribosomal RNA Modification Enzymes : Structural and functional studies of two methyltransferases for 23S rRNA modification in Escherichia coli

   Author : Avinash S. Punekar; Maria Selmer; Martino Bolognesi; Uppsala universitet; []
   Keywords : NATURVETENSKAP; NATURAL SCIENCES; NATURVETENSKAP; NATURAL SCIENCES; Escherichia coli; ribosome biogenesis; ribosome assembly; ribosomal RNA; peptidyltransferase center; domain V; post-transcriptional modification; methyltransferases; S-adenosyl-methionine; RlmM; Cm2498; RlmJ; m6A2030; X-ray crystallography; substrate recognition; substrate specificity; catalytic mechanism; evolution; Biology with specialization in Structural Biology; Biologi med inriktning mot strukturbiologi; Biokemi; Biochemistry;

   Abstract : Escherichia coli ribosomal RNA (rRNA) is post-transcriptionally modified by site-specific enzymes. The role of most modifications is not known and little is known about how these enzymes recognize their target substrates. READ MORE

6. 4. Structure-Function Relationships of Pi Class Glutathione Transferase Studied by Protein Engineering

   Author : Usama M. Hegazy; Bengt Mannervik; Mikael Widersten; T. J. Mantle; Uppsala universitet; []
   Keywords : Biochemistry; Glutathione transferase; targeted chemical modification; lock-and-key motif; cooperativity; stucture-function relationship; protein engineering; unnatural amino acid; site-specific mutation; Biokemi;

   Abstract : The glutathione transferases (GSTs) represent a superfamily of dimeric proteins involved in cellular detoxication by catalyzing the nucleophilic addition of the reduced glutathione (GSH) to the hydrophobic electrophiles. The present work focuses on the functional role of the conserved structures of GSTP1-1. READ MORE

7. 5. A Novel Route for Construction of Multipurpose Receptors through Chemical Modification of Glutathione Transferases

   Author : Johan Viljanen; Bengt Harald Jonsson; Kerstin Broo; Sophia Hober; Linköpings universitet; []
   Keywords : NATURVETENSKAP; NATURAL SCIENCES; Human GST A1-1; site-specific covalent modification; tyrosine 9; lysine 216; methionine 208; multipurpose receptor; pattern recognition; protein purification; Chemistry; Kemi;

   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