Search for dissertations about: "Conformational entropy change"

Showing result 1 - 5 of 7 swedish dissertations containing the words Conformational entropy change.

2. 1. Molecular recognition and dynamics in proteins studied by NMR

   Author : Johan Wallerstein; Biofysikalisk kemi; []
   Keywords : NATURVETENSKAP; NATURAL SCIENCES; NATURVETENSKAP; NATURAL SCIENCES; Chemical exchange; Conformational entropy; Entropy; Galectin-3; Isothermal Titration Calorimetry; ITC; Model-free formalism; Molecular recognition; Nuclear Magnetic Resonance; NMR; PGB1; Protein dynamics; Protein–ligand interactions; Proton-transfer reactions; Spin relaxation; Viscosity; Chemical exchange; Conformational entropy; Entropy; Galectin-3; Isothermal Titration Calorimetry; ITC; Model-free formalism; Molecular recognition; Nuclear Magnetic Resonance; NMR; PGB1; Protein dynamics; Protein–ligand interactions; Proton-transfer reactions; Spin relaxation; Viscosity;

   Abstract : Knowledge of dynamics in protein is very important in the description of protein function and molecular recognition. The thesis investigates protein dynamics on time-scales from milli- to sub-nanosecond, with focus on the latter, using NMR spin relaxation experiments on two proteins, the 138-residue carbohydrate recognition domain of galectin-3 (Gal3C) and the 56-residue B1 domain of bacterial protein G (PGB1). READ MORE

4. 2. Conformational Entropy and Protein Flexibility in Drug Design Studied by NMR Spectroscopy

   Author : Carl Diehl; Biofysikalisk kemi; []
   Keywords : NATURVETENSKAP; NATURAL SCIENCES; MMP-12; Galectin-3; confomational entropy; order parameters; ITC; Protein dynamics; isothermal titration calorimetry; macrophage elastase; nuclear magnetic resonance; NMR;

   Abstract : Proteins are complex molecules, present in all of the vital functions of life. The function of a protein is regulated by interactions between protein and other molecules. Drug design in pharmaceutical science aims to regulate the function of a protein by the design of synthesized molecules that binds to a protein with high affinity. READ MORE

5. 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

6. 4. Design, Synthesis and Thermodynamic Studies of Galectin Ligands

   Author : Maria Luisa Verteramo; Centrum för analys och syntes; []
   Keywords : NATURVETENSKAP; NATURAL SCIENCES; TEKNIK OCH TEKNOLOGIER; ENGINEERING AND TECHNOLOGY; galectin; conformational entropy; solvation; thermodynamic; interaction; molecular recognition; thiodigalactoside; diastereomer; structure-based design;

   Abstract : The signaling within and between cells in biology is governed by molecular recognition between natural or synthetic ligands and proteins. This thesis project aimed to investigate the thermodynamic properties of specific interaction between synthetic ligands and galectin proteins. READ MORE

7. 5. Structure determination and thermodynamic stabilization of an engineered protein-protein complex

   Author : Elisabet Wahlberg; Per-Åke Nygren; Bengt-Harald Jonsson; KTH; []
   Keywords : TEKNIK OCH TEKNOLOGIER; ENGINEERING AND TECHNOLOGY; affibody; protein structure; coupled folding; NMR spectroscopy; protein stability; protein-protein interactions; binding thermodynamics; isothermal titration calorimetry; protein engineering; Structural biochemistry; Strukturbiokemi;

   Abstract : The interaction between two 6 kDa proteins has been investigated. The studied complex of micromolar affinity (Kd) consists of the Z domain derived from staphylococcal protein A and the related protein ZSPA-1, belonging to a group of binding proteins denoted affibody molecules generated via combinatorial engineering of the Z domain. READ MORE