Protein Structure and Dynamics – Lukáš Žídek

• Structure, dynamics and interactions of proteins
• Intrinsically disordered proteins
• Development and application of NMR methodology

• Development of new methodologies for the investigation of biomolecular structures, interactions, and dynamics.
• Investigations of the biomolecular structures and interactions and their relationship with physiological functions, diseases and therapies.
• Production of pure and homogeneous proteins for the structural analysis.
• Production of monoclonal antibodies, with emphasis on the quality of the antigen – antibody selection.  Selection of binding molecules from synthetic DNA libraries for diagnostic and therapeutic use.

Our group is interested in structure, dynamics, interactions, and function of proteins. Currently, our major focus is proteins containing intrinsically disordered regions. Due to the presence of the intrinsically disordered regions, nuclear magnetic resonance (NMR) plays an important role in detailed characterization of the studied proteins. In addition to conventional NMR methods, we have developed approaches allowing us to study large disordered proteins with atomic-resolution. We combine NMR spectroscopy with cryo-electron microscopy to describe interactions of the investigated proteins and their complexes at conditions close to their natural environment. Currently, we study mostly two types of biological systems: (1) proteins regulating bacterial transcription and (2) microtubule-associated proteins of brain neurons and their interacting partners.