Sökning: "Structural stability"

Visar resultat 16 - 20 av 547 avhandlingar innehållade orden Structural stability.

  1. 16. Molecular principles of protein stability and protein-protein interactions

    Författare :Christofer Lendel; Per-Åke Nygren; Christopher M. Dobson; KTH; []
    Nyckelord :TEKNIK OCH TEKNOLOGIER; ENGINEERING AND TECHNOLOGY; affibody; binding thermodynamics; induced fit; molten globule; NMR spectroscopy; protein engineering; protein-protein interactions; protein stability; protein structure.; Structural biochemistry; Strukturbiokemi;

    Sammanfattning : Proteins with highly specific binding properties constitute the basis for many important applications in biotechnology and medicine. Immunoglobulins have so far been the obvious choice but recent advances in protein engineering have provided several novel constructs that indeed challenge antibodies. LÄS MER

  2. 17. Transaminase Biocatalysis: Applications and Fundamental Studies

    Författare :Federica Ruggieri; Per Berglund; Mariarita Bertoldi; KTH; []
    Nyckelord :TEKNIK OCH TEKNOLOGIER; ENGINEERING AND TECHNOLOGY; biocatalysis; enzymatic cascade; transaminase; amine; racemization; PLP; enzyme engineering; Chromobacterium violaceum; protein stability; enzyme stability; molecular dynamics; structural biology; enzyme technology; chiral amines; kinetic resolution; Bioteknologi; Biotechnology;

    Sammanfattning : Biocatalysis is the branch of science at the intersection between chemistry and biology and specifcally dedicated to the application of natural evolvable catalysts, i.e. enzymes, in human-designed chemical processes. Among the array of promising biocatalysts, transaminases (EC 2. LÄS MER

  3. 18. Structural and thermodynamical basis for molecular recognition between engineered binding proteins

    Författare :Jakob Dogan; Per-Åke Nygren; John E. Ladbury; KTH; []
    Nyckelord :TEKNIK OCH TEKNOLOGIER; ENGINEERING AND TECHNOLOGY; protein structure; induced fit; binding thermodynamics; NMR spectroscopy; protein engineering; protein-protein interactions; protein stability; calorimetry; Structural biochemistry; Strukturbiokemi;

    Sammanfattning : The structural determination of interacting proteins, both as individual proteins and in their complex, complemented by thermodynamical studies are vital in order to gain in-depth insights of the phenomena leading to the highly selective protein-protein interactions characteristic of numerous life processes. This thesis describes an investigation of the structural and thermodynamical basis for molecular recognition in two different protein-protein complexes, formed between so-called affibody proteins and their respective targets. LÄS MER

  4. 19. Thiopurine S-methyltransferase - characterization of variants and ligand binding

    Författare :Annica Blissing; Lars-Göran Mårtensson; Tomas Nyman; Linköpings universitet; []
    Nyckelord :NATURVETENSKAP; NATURAL SCIENCES; NATURVETENSKAP; NATURAL SCIENCES; MEDICIN OCH HÄLSOVETENSKAP; MEDICAL AND HEALTH SCIENCES; MEDICIN OCH HÄLSOVETENSKAP; MEDICAL AND HEALTH SCIENCES; TEKNIK OCH TEKNOLOGIER; ENGINEERING AND TECHNOLOGY; NATURVETENSKAP; NATURAL SCIENCES; Thiopurine S-methyltransferase TPMT ; protein stability; enzyme kinetics; ligand binding; isothermal titration calorimetry ITC ; 8-anilinonaphthalene-1-sulfonic acid ANS ;

    Sammanfattning : Thiopurine S-methyltransferase (TPMT) belongs to the Class I S-adenosylmethionine-dependent methyltransferase (SAM-MT) super family of structurally related proteins. Common to the members of this large protein family is the catalysis of methylation reactions using S-adenosylmethionine (SAM) as a methyl group donor, although SAM-MTs act on a wide range of different substrates and carry out numerous biologically important functions. LÄS MER

  5. 20. The Design and Structure Prediction of Protein Oligomers

    Författare :Robert Lizatovic; Biokemi och Strukturbiologi; []
    Nyckelord :NATURVETENSKAP; NATURAL SCIENCES; NATURVETENSKAP; NATURAL SCIENCES; virus capsids; coiled coils; molecular replacement; symmetry; Rosetta; protein design; structure prediction;

    Sammanfattning : The minimum free energy state of a protein (the native state) is encoded by its amino-acid sequence. Due to the many torsional degrees of freedom (DOF) available to a polypeptide chain, a vast number of conformations is possible. LÄS MER