Search for dissertations about: "protein-protein interactions"

Showing result 1 - 5 of 186 swedish dissertations containing the words protein-protein interactions.

  1. 1. Antiadhesive agents targeting uropathogenic Escherichia coli : Multivariate studies of protein-protein and protein-carbohydrate interactions

    Author : Andreas Larsson; Jan Kihlberg; Fredrik Almqvist; Mats Larhed; Umeå universitet; []
    Keywords : NATURVETENSKAP; NATURAL SCIENCES; Organic chemistry; Antibacterial; pili; antiadhesive agents; structure based design; statistical molecular design; 2-pyridone; amino acid derivative; galabiose; enaminone; SPR; ELISA; QSAR; Organisk kemi; Organic chemistry; Organisk kemi; organisk kemi; Organic Chemistry;

    Abstract : This thesis describes studies directed towards development of novel antiadhesive agents, with particular emphasis on compounds that prevent attachment of bacteria to a host-cell. Three different proteins involved in the assembly or function of adhesive pili in uropathogenic Escherichia coli have been targeted either by rational structure based design or statistical molecular methods. READ MORE

  2. 2. Protein-Protein Interactions in Human Aquaporin Regulation

    Author : Jennifer Virginia Roche; Biokemi och Strukturbiologi; []
    Keywords : NATURVETENSKAP; NATURAL SCIENCES; NATURVETENSKAP; NATURAL SCIENCES; Membrane proteins; Human Aquaporins; water channels; Protein-protein interaction; Regulation; AQP2; AQP0; LIP5; CaM;

    Abstract : Water is an essential compoment of every living orgamism and forms a major part of the human body. Regulated water transport is crucial for proper cell functioning and body homeostasis. READ MORE

  3. 3. Biophysical characterization of protein-protein interactions involving intrinsically disordered proteins

    Author : Ida Nyqvist; Jakob Dogan; Ivarsson Ylva; Stockholms universitet; []
    Keywords : NATURVETENSKAP; NATURAL SCIENCES; Intrinsically disordered proteins; Protein-protein interactions; Disorder-to-order transition; Rate-limiting transition state; Ф-value analysis; NMR relaxation; Side-chain dynamics; Backbone dynamics; Conformational entropy change; Biophysics; biofysik;

    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

  4. 4. Intra- and intermolecular interactions in proteins : Studies of marginally hydrophobic transmembrane alpha-helices and protein-protein interactions

    Author : Linnea E Hedin; Arne Elofsson; Susana Cristobal; Ismael Mingarro; Stockholms universitet; []
    Keywords : NATURVETENSKAP; NATURAL SCIENCES; membrane proteins; membrane insertion; marginally hydrophobic helix; hydrophobicity; protein-protein interactions; LacY; GltPh; Cell and molecular biology; Cell- och molekylärbiologi; Biochemistry; Biokemi; Biochemistry; biokemi;

    Abstract : Most of the processes in a living cell are carried out by proteins. Depending on the needs of the cell, different proteins will interact and form the molecular machines demanded for the moment. READ MORE

  5. 5. Protein-protein interactions in model systems : design, control of catalytic activity and biosensor applications

    Author : Johan Rydberg; Lars Baltzer; Joel Schneider; Linköpings universitet; []
    Keywords : NATURVETENSKAP; NATURAL SCIENCES; Chemistry; Protein interactions; design; catalysis; biosensors; hybride materials; nanoparticles; Kemi; Chemistry; Kemi;

    Abstract : This thesis describes the design of polypeptides, unordered in the monomeric state but capable of folding into helix-loop-helix motifs and dimerise to form four-helix bundles. The goal of the design was to encode them with the capacity to form dimers highly selectively and the ability to carry out molecular functions in the folded state but not in the unordered state, and thus to establish a molecular link between recognition and function. READ MORE