Search for dissertations about: "intrinsically disordered protein regions"
Showing result 1 - 5 of 21 swedish dissertations containing the words intrinsically disordered protein regions.
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1. Biophysical characterization of protein-protein interactions involving intrinsically disordered proteins
Abstract : Intrinsically disordered proteins and regions (IDPs/Rs) are proteins that do not form stable and well-defined structures in their free states but rather occupy an ensemble of conformations that change over time while still staying functional. They are prevalent in the eukaryotic proteome and are involved in various vital processes in the cell where they often interact with their binding partners through coupled binding and folding reactions. READ MORE
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2. Variation in length of proteins by repeats and disorder regions
Abstract : Protein-coding genes evolve together with their genome and acquire changes, some of which affect the length of their protein products. This explains why equivalent proteins from different species can exhibit length differences. READ MORE
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3. Characterization and Engineering of Protein-Protein Interactions Involving PDZ Domains
Abstract : The work presented in this thesis has contributed with knowledge to several aspects of protein-protein interaction involving PDZ domains. A substantial amount of our proteome contains regions that are intrinsically disordered but fold upon ligand interaction. READ MORE
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4. Evolution and Binding Mechanisms of Intrinsically Disordered Proteins
Abstract : Intrinsically disordered proteins (IDPs) make up a considerable fraction of the proteome in eukaryotic organisms. These proteins often act as hubs in interaction networks, harbouring multiple interaction with other proteins, and thus evolution has to walk a tightrope to accommodate new interactions while maintaining the previously established interactions. READ MORE
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5. From protein sequence to structural instability and disease
Abstract : A great challenge in bioinformatics is to accurately predict protein structure and function from its amino acid sequence, including annotation of protein domains, identification of protein disordered regions and detecting protein stability changes resulting from amino acid mutations. The combination of bioinformatics, genomics and proteomics becomes essential for the investigation of biological, cellular and molecular aspects of disease, and therefore can greatly contribute to the understanding of protein structures and facilitating drug discovery. READ MORE