Karin Hauser
Protein structure formation studied by time-resolved infrared spectroscopy
We develop time-resolved infrared spectroscopic techniques to study the molecular mechanisms of protein folding, misfolding and aggregation, processes which essentially determine cellular proteostasis. One major goal in this project focuses on β-sheet formation and polyQ-mediated fibril initiation (in collaboration with A01). Particular interest in understanding the factors affecting β-sheet formation is prompted by the fact that many degenerative diseases have their pathology rooted in protein or peptide aggregation which often involves β-sheet formation. Another major goal focuses on the Parkinson´s Disease protein α-synuclein (ASYN) and the importance of the membrane interaction (in collaboration with C03 and C05). Membrane integrity and structural changes of ASYN are probed simultaneously at the protein-membrane interface and in a time-resolved manner. The effect of posttranslational modifications on ASYN binding and aggregation will be explored on a molecular level.