Structural and Functional Studies of Proteins Involved in the Regulation of Fatty Acid Metabolism

Abstract

The Doctoral Thesis is devoted to structure-activity relationship studies of γ-butyrobetaine dioxygenase, ε-trimethyl-l-lysine dioxygenase (TMLD), and heart-type fatty acid binding protein (FABP3) ligands. Protein-ligand binding was determined and characterized by means of isothermal titration calorimetry (ITC), nuclear magnetic resonance, and molecular modelling. Two new ITC approaches were established and implemented for the determination of ligand binding thermodynamics to TMLD and FABP3. A new class of FABP3 substrates with a different binding mechanism in comparison to fatty acids was found.