Biophysical and Structural Characterisation of Helicobacter pylori Motility and Chemotaxis Proteins

This study focuses on understanding the structure and function of H. pylori's motility and chemotaxis proteins, crucial for its survival and infectivity, and identifying new drug targets. The first part of the thesis focuses on purifying six newly discovered H. pylori scaffold candidate proteins and examining how they interact with the motility protein MotB and with each other, using Surface Plasmon Resonance technology. The second part of this thesis delves into the chemotaxis protein TlpC, looking at its structure when bound with its ligand and employing biophysical assays, including Isothermal Titration Calorimetry and Thermal Shift Assay to study ligand-protein interactions.