Time-Resolved Structural Biology
Protein function is critically dependent on coordinated motions induced by interactions with ligands, other proteins or changes in environment. Insights into the complex structures of proteins and knowledge of protein motions throughout their conformational landscape have tremendous impact on biology. The dynamic interaction between ligands and their protein partners is the molecular basis for pharmacological intervention in human disease.
We are using cutting edge X-ray technologies to track ligand-protein interactions over time and resolve conformational states important for protein function. To achieve this aim, we establish time-resolved serial crystallography at the Swiss Light Source (SLS) and the Swiss Free Electron Laser (SwissFEL). Structural snapshots are complemented with spectroscopy and computational simulations to provide clear cause-and-effect descriptions of stepwise structural rearrangements in a range of protein targets including membrane pumps and G protein-coupled receptors.
Jörg Standfuss, Laboratory Head and Group leader
Integrative structural biology of dynamic systems
Tobias Weinert, Scientist
Serial crystallography
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