Sökning: "Conformational entropy change"
Visar resultat 1 - 5 av 7 avhandlingar innehållade orden Conformational entropy change.
Sammanfattning : 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). LÄS MER
Sammanfattning : 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. LÄS MER
3. Biophysical characterization of protein-protein interactions involving intrinsically disordered proteins
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
Sammanfattning : 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. LÄS MER
Sammanfattning : 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. LÄS MER