Sökning: "backbone dynamics"

Visar resultat 1 - 5 av 60 avhandlingar innehållade orden backbone dynamics.

  1. 1. Protein-water interactions studied by molecular dynamics simulations

    Författare :Filip Persson; Biofysikalisk kemi; []
    Nyckelord :NATURVETENSKAP; NATURAL SCIENCES; NATURVETENSKAP; NATURAL SCIENCES; MD simulations; NMR nuclear magnetic resonance ; MRD; water dynamics; protein dynamics; protein hydration; Amide hydrogen exchange; Internal water; compressibility;

    Sammanfattning : Most proteins have evolved to function optimally in aqueous environments, and the interactions between protein and water therefore play a fundamental role in the stability, dynamics, and function of proteins. Although we understand many details of water, we understand much less about the protein-water interface. LÄS MER

  2. 2. Shaking the EF-Hand. Dynamics and Ion-Binding to Calmodulin and Calbindin D9k

    Författare :Anders Malmendal; Biofysikalisk kemi; []
    Nyckelord :NATURVETENSKAP; NATURAL SCIENCES; magnesium; line shape; ion binding; EF-hand; cooperativity; conformational exchange; chemical shift; calmodulin; calcium; calbindin D9k; allostery; backbone dynamics; NMR; relaxation; Physical chemistry; Fysikalisk kemi;

    Sammanfattning : The work described in this thesis represents a biophysical approach, mainly using nuclear magnetic resonance (NMR) spectroscopy, to investigate the impact of magnesium ions on the EF-hand calcium-binding proteins calmodulin and calbindin D9k, as well as the dynamics of these proteins at low calcium levels. The x-ray structure of magnesium-saturated calbindin D9k shows a magnesium ion in only one of the two ion binding sites. LÄS MER

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

    Författare :Ida Nyqvist; Jakob Dogan; Ivarsson Ylva; Stockholms universitet; []
    Nyckelord :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;

    Sammanfattning : 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. LÄS MER

  4. 4. Taming the Griffin : Membrane interactions of peripheral and monotopic glycosyltransferases and dynamics of bacterial and plant lipids in bicelles

    Författare :Jobst Liebau; Lena Mäler; Charles Sanders; Stockholms universitet; []
    Nyckelord :NATURVETENSKAP; NATURAL SCIENCES; membrane; bicelle; lipid; detergent; lipopolysaccharide; glycosyltransferase; WaaG; fluorescence; circular dichroism; NMR; paramagnetic relaxation enhancement; model-free approach; dynamics; Biophysics; biofysik;

    Sammanfattning : Biological membranes form a protective barrier around cells and cellular compartments. A broad range of biochemical processes occur in or at membranes demonstrating that they are not only of structural but also of functional importance. One important class of membrane proteins are membrane-associated glycosyltransferases. LÄS MER

  5. 5. Molecular dynamics studied by NMR relaxation experiments. Characterization of functional dynamics in the FK506 binding protein FKBP12

    Författare :Ulrika Brath; Biofysikalisk kemi; []
    Nyckelord :NATURVETENSKAP; NATURAL SCIENCES; nuclear magnetic resonance; NMR; FK506; protein dynamics; chemical exchange; spin relaxation; FKBP12; FKBP; isotope labeling;

    Sammanfattning : The presented thesis work is concerned with the study of molecular dynamics using liquid nuclear magnetic resonance (NMR) spectroscopy. Spin relaxation dispersion experiments in the rotating frame (R1ρ) are employed to provide a detailed, atomic-resolution view of protein dynamics. LÄS MER